P04114 (APOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Apolipoprotein B-100
Short name=Apo B-100

Cleaved into the following chain:

1. Apolipoprotein B-48
   Short name=Apo B-48

Gene names

Name:

APOB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	4563 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	Interacts with PCSK9. Ref.38
Subcellular location	Cytoplasm. Secreted Ref.38.
Induction	Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.34
Post-translational modification	Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle. Ref.31
Involvement in disease	Familial hypobetalipoproteinemia 1 (FHBL1) [MIM:107730]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.46 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.42 Ref.44 Ref.49 Defects in APOB associated with defects in other genes (polygenic) can contribute to hypocholesterolemia.
Sequence similarities	Contains 1 vitellogenin domain.
RNA editing	Edited at position 2180. 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.
Sequence caution	The sequence AAA51752.1 differs from that shown. Reason: Frameshift at positions 942, 951, 1139, 1165, 1164, 1371 and 1385.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Lipid transport Steroid metabolism Sterol metabolism Transport
Cellular component	Chylomicron Cytoplasm LDL Secreted VLDL
Coding sequence diversity	Polymorphism RNA editing
Disease	Atherosclerosis Disease mutation
Domain	Signal
Ligand	Heparin-binding
PTM	Acetylation Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	artery morphogenesis Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome cellular response to prostaglandin stimulus Inferred from electronic annotation. Source: Compara cellular response to tumor necrosis factor Inferred from electronic annotation. Source: Compara cholesterol efflux Inferred from electronic annotation. Source: Compara cholesterol homeostasis Inferred from mutant phenotype Ref.40. Source: BHF-UCL cholesterol metabolic process Inferred from mutant phenotype Ref.40. Source: BHF-UCL fertilization Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara leukocyte migration Traceable author statement. Source: Reactome lipoprotein biosynthetic process Inferred from electronic annotation. Source: Compara lipoprotein catabolic process Inferred from electronic annotation. Source: Compara lipoprotein metabolic process Traceable author statement. Source: Reactome lipoprotein transport Inferred from electronic annotation. Source: Compara low-density lipoprotein particle clearance Inferred from mutant phenotype PubMed 15797858Ref.40. Source: BHF-UCL low-density lipoprotein particle remodeling Inferred from mutant phenotype PubMed 15797858. Source: BHF-UCL nervous system development Inferred from electronic annotation. Source: Compara positive regulation of cholesterol storage Inferred from direct assay PubMed 19114110. Source: BHF-UCL positive regulation of macrophage derived foam cell differentiation Inferred from direct assay PubMed 17244792PubMed 18322245PubMed 19114110. Source: BHF-UCL post-embryonic development Inferred from electronic annotation. Source: Compara receptor-mediated endocytosis Traceable author statement. Source: Reactome regulation of cholesterol biosynthetic process Inferred from electronic annotation. Source: Compara response to carbohydrate stimulus Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to selenium ion Inferred from electronic annotation. Source: Compara response to virus Inferred from expression pattern Ref.34. Source: UniProtKB sperm motility Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara triglyceride catabolic process Inferred from electronic annotation. Source: Compara triglyceride mobilization Inferred from electronic annotation. Source: Compara very-low-density lipoprotein particle assembly Inferred by curator PubMed 15308631. Source: BHF-UCL
Cellular_component	chylomicron remnant Traceable author statement PubMed 6099394. Source: BHF-UCL clathrin-coated endocytic vesicle membrane Traceable author statement. Source: Reactome endoplasmic reticulum lumen Traceable author statement. Source: Reactome endoplasmic reticulum membrane Traceable author statement. Source: Reactome endosome lumen Traceable author statement. Source: Reactome endosome membrane Traceable author statement. Source: Reactome intermediate-density lipoprotein particle Inferred from direct assay PubMed 1917954. Source: BHF-UCL low-density lipoprotein particle Inferred from direct assay PubMed 4363408. Source: BHF-UCL mature chylomicron Inferred from direct assay PubMed 4363408. Source: BHF-UCL plasma membrane Traceable author statement. Source: Reactome very-low-density lipoprotein particle Inferred from direct assay PubMed 15308631PubMed 4363408. Source: BHF-UCL vesicle lumen Inferred from electronic annotation. Source: Compara
Molecular_function	cholesterol transporter activity Inferred from mutant phenotype PubMed 15797858. Source: BHF-UCL heparin binding Inferred from direct assay PubMed 16233946. Source: BHF-UCL low-density lipoprotein particle receptor binding Inferred from mutant phenotype PubMed 15797858Ref.40. Source: BHF-UCL phospholipid binding Inferred from direct assay PubMed 7126555. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27
	Chain	28 – 4563	4536	Apolipoprotein B-100		PRO_0000020750
	Chain	28 – 2179	2152	Apolipoprotein B-48		PRO_0000020751
Regions
	Domain	46 – 672	627	Vitellogenin
	Region	32 – 126	95	Heparin-binding
	Region	232 – 306	75	Heparin-binding
	Region	902 – 959	58	Heparin-binding
	Region	2043 – 2178	136	Heparin-binding
	Region	3161 – 3236	76	Heparin-binding
	Region	3174 – 3184	11	Basic (possible receptor binding region)
	Region	3373 – 3393	21	LDL receptor binding
	Region	3383 – 3516	134	Heparin-binding
	Region	3386 – 3394	9	Basic (possible receptor binding region)
Amino acid modifications
	Modified residue	2004	1	N6-acetyllysine Ref.36
	Lipidation	1112	1	S-palmitoyl cysteine Ref.31
	Glycosylation	34	1	N-linked (GlcNAc...) Potential
	Glycosylation	185	1	N-linked (GlcNAc...) Ref.35
	Glycosylation	983	1	N-linked (GlcNAc...) Potential
	Glycosylation	1368	1	N-linked (GlcNAc...) Potential
	Glycosylation	1377	1	N-linked (GlcNAc...) Potential
	Glycosylation	1523	1	N-linked (GlcNAc...) Ref.33 Ref.35
	Glycosylation	2239	1	N-linked (GlcNAc...) Ref.35
	Glycosylation	2560	1	N-linked (GlcNAc...) Potential
	Glycosylation	2779	1	N-linked (GlcNAc...) Ref.35
	Glycosylation	2982	1	N-linked (GlcNAc...) Ref.33 Ref.35
	Glycosylation	3101	1	N-linked (GlcNAc...) Ref.35
	Glycosylation	3224	1	N-linked (GlcNAc...) Ref.35
	Glycosylation	3336	1	N-linked (GlcNAc...) Potential
	Glycosylation	3358	1	N-linked (GlcNAc...) Ref.32
	Glycosylation	3411	1	N-linked (GlcNAc...) Ref.35
	Glycosylation	3465	1	N-linked (GlcNAc...) Ref.33 Ref.35
	Glycosylation	3895	1	N-linked (GlcNAc...) Ref.33 Ref.35
	Glycosylation	4237	1	N-linked (GlcNAc...) Potential
	Glycosylation	4431	1	N-linked (GlcNAc...) Potential
	Disulfide bond	39 ↔ 88		Ref.10
	Disulfide bond	78 ↔ 97		Ref.10
	Disulfide bond	186 ↔ 212		Ref.10
	Disulfide bond	245 ↔ 261		Ref.10
	Disulfide bond	385 ↔ 390		Ref.10
	Disulfide bond	478 ↔ 513		Ref.10
	Disulfide bond	966 ↔ 976		Ref.10
	Disulfide bond	3194 ↔ 3324		Ref.10
Natural variations
	Natural variant	12 – 14	3	Missing.		VAR_067277
	Natural variant	98	1	T → I. Ref.3 Ref.8 Ref.10 Ref.46 Ref.51 Corresponds to variant rs1367117 [ dbSNP | Ensembl ].		VAR_016184
	Natural variant	103	1	Y → H. Corresponds to variant rs9282603 [ dbSNP | Ensembl ].		VAR_022036
	Natural variant	145	1	P → S. Corresponds to variant rs6752026 [ dbSNP | Ensembl ].		VAR_022037
	Natural variant	194	1	T → M. Corresponds to variant rs13306198 [ dbSNP | Ensembl ].		VAR_056737
	Natural variant	273	1	K → N. Ref.1 Corresponds to variant rs1126419 [ dbSNP | Ensembl ].		VAR_019827
	Natural variant	408	1	I → T. Corresponds to variant rs12714225 [ dbSNP | Ensembl ].		VAR_029341
	Natural variant	490	1	R → W in FHBL1; reduced protein secretion. Ref.46		VAR_022610
	Natural variant	554	1	P → L. Corresponds to variant rs12714214 [ dbSNP | Ensembl ].		VAR_020135
	Natural variant	618	1	A → V. Ref.3 Ref.5 Ref.51 Corresponds to variant rs679899 [ dbSNP | Ensembl ].		VAR_019828
	Natural variant	730	1	V → I. Ref.51 Corresponds to variant rs12691202 [ dbSNP | Ensembl ].		VAR_020136
	Natural variant	733	1	V → I. Corresponds to variant rs1800476 [ dbSNP | Ensembl ].		VAR_016185
	Natural variant	741	1	T → N. Corresponds to variant rs12714192 [ dbSNP | Ensembl ].		VAR_020137
	Natural variant	877	1	P → L. Corresponds to variant rs12714097 [ dbSNP | Ensembl ].		VAR_029342
	Natural variant	955	1	P → S. Corresponds to variant rs13306206 [ dbSNP | Ensembl ].		VAR_056738
	Natural variant	1086	1	G → S. Corresponds to variant rs12720801 [ dbSNP | Ensembl ].		VAR_029343
	Natural variant	1113	1	D → H. Corresponds to variant rs12713844 [ dbSNP | Ensembl ].		VAR_029344
	Natural variant	1128	1	R → H. Ref.47 Corresponds to variant rs12713843 [ dbSNP | Ensembl ].		VAR_022611
	Natural variant	1218	1	Q → E Polymorphism confirmed at protein level. Ref.1 Ref.50 Corresponds to variant rs1041956 [ dbSNP | Ensembl ].		VAR_019829
	Natural variant	1388	1	R → H. Corresponds to variant rs13306187 [ dbSNP | Ensembl ].		VAR_029345
	Natural variant	1422	1	Y → C. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.15 Corresponds to variant rs568413 [ dbSNP | Ensembl ].		VAR_061558
	Natural variant	1437	1	F → L. Ref.43 Corresponds to variant rs1801697 [ dbSNP | Ensembl ].		VAR_005016
	Natural variant	1613	1	S → T. Ref.51		VAR_067278
	Natural variant	1670	1	E → D Polymorphism confirmed at protein level. Ref.8 Ref.50		VAR_068911
	Natural variant	1914	1	N → S. Ref.43 Ref.45 Corresponds to variant rs1801699 [ dbSNP | Ensembl ].		VAR_005017
	Natural variant	1923	1	H → R. Ref.45 Ref.51 Corresponds to variant rs533617 [ dbSNP | Ensembl ].		VAR_005018
	Natural variant	2037	1	I → N Polymorphism confirmed at protein level. Ref.4 Ref.50		VAR_068912
	Natural variant	2092	1	L → V. Ref.1 Corresponds to variant rs1041960 [ dbSNP | Ensembl ].		VAR_019830
	Natural variant	2299	1	D → H. Corresponds to variant rs12713681 [ dbSNP | Ensembl ].		VAR_029346
	Natural variant	2313	1	I → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.15 Ref.16 Corresponds to variant rs584542 [ dbSNP | Ensembl ].		VAR_059582
	Natural variant	2365	1	A → T. Ref.1 Corresponds to variant rs1041971 [ dbSNP | Ensembl ].		VAR_019831
	Natural variant	2456	1	A → D. Corresponds to variant rs12713675 [ dbSNP | Ensembl ].		VAR_020138
	Natural variant	2564	1	F → C in a colorectal cancer sample; somatic mutation; polymorphism confirmed at protein level. Ref.48 Ref.50		VAR_035795
	Natural variant	2566	1	E → K Polymorphism confirmed at protein level. Ref.43 Ref.50 Ref.51 Corresponds to variant rs1801696 [ dbSNP | Ensembl ].		VAR_005019
	Natural variant	2680	1	L → Q. Ref.1 Corresponds to variant rs1042013 [ dbSNP | Ensembl ].		VAR_019832
	Natural variant	2739	1	P → L. Ref.41 Ref.45 Ref.51 Corresponds to variant rs676210 [ dbSNP | Ensembl ].		VAR_005020
	Natural variant	2785	1	N → H. Corresponds to variant rs2163204 [ dbSNP | Ensembl ].		VAR_022038
	Natural variant	3121	1	A → T. Ref.43 Corresponds to variant rs1801694 [ dbSNP | Ensembl ].		VAR_005021
	Natural variant	3182	1	H → N. Corresponds to variant rs12720848 [ dbSNP | Ensembl ].		VAR_029347
	Natural variant	3279	1	S → G. Corresponds to variant rs12720854 [ dbSNP | Ensembl ].		VAR_029348
	Natural variant	3294	1	S → P. Corresponds to variant rs12720855 [ dbSNP | Ensembl ].		VAR_020139
	Natural variant	3319	1	D → H. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.15 Ref.23 Ref.45		VAR_005022
	Natural variant	3427	1	T → K. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.15 Ref.23 Ref.45		VAR_005023
	Natural variant	3432	1	Q → E. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.15 Ref.23 Ref.45 Corresponds to variant rs1042023 [ dbSNP | Ensembl ].		VAR_005024
	Natural variant	3527	1	R → Q in FDB. Ref.40 Ref.44 Ref.49 Corresponds to variant rs5742904 [ dbSNP | Ensembl ].		VAR_005025
	Natural variant	3558	1	R → C in FDB. Ref.42 Ref.44 Corresponds to variant rs12713559 [ dbSNP | Ensembl ].		VAR_005026
	Natural variant	3638	1	R → Q. Ref.51 Corresponds to variant rs1801701 [ dbSNP | Ensembl ].		VAR_016186
	Natural variant	3732	1	I → T. Ref.1 Ref.5 Ref.15 Ref.23 Corresponds to variant rs1042025 [ dbSNP | Ensembl ].		VAR_019833
	Natural variant	3801	1	S → T. Corresponds to variant rs12713540 [ dbSNP | Ensembl ].		VAR_029349
	Natural variant	3835	1	I → L. Ref.51		VAR_067279
	Natural variant	3921	1	V → I. Ref.45		VAR_005027
	Natural variant	3945	1	T → A. Ref.43 Corresponds to variant rs1801698 [ dbSNP | Ensembl ].		VAR_005028
	Natural variant	3949	1	F → L. Ref.1 Ref.4 Ref.5 Ref.23 Ref.25 Corresponds to variant rs1042027 [ dbSNP | Ensembl ].		VAR_019834
	Natural variant	3964	1	Y → F. Ref.1 Ref.5 Ref.23 Ref.25 Corresponds to variant rs1126468 [ dbSNP | Ensembl ].		VAR_019835
	Natural variant	4128	1	V → M. Ref.43 Corresponds to variant rs1801703 [ dbSNP | Ensembl ].		VAR_005029
	Natural variant	4181	1	E → K. Ref.1 Ref.4 Ref.5 Ref.23 Ref.25 Ref.51 Corresponds to variant rs1042031 [ dbSNP | Ensembl ].		VAR_016187
	Natural variant	4270	1	R → T. Ref.51 Corresponds to variant rs1801702 [ dbSNP | Ensembl ].		VAR_016188
	Natural variant	4314	1	I → V. Ref.51		VAR_067280
	Natural variant	4338	1	S → N. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.15 Ref.23 Ref.24 Ref.39 Ref.51 Corresponds to variant rs1042034 [ dbSNP | Ensembl ].		VAR_005030
	Natural variant	4394	1	V → A. Corresponds to variant rs12720843 [ dbSNP | Ensembl ].		VAR_029350
	Natural variant	4481	1	A → T. Ref.43 Ref.51 Corresponds to variant rs1801695 [ dbSNP | Ensembl ].		VAR_005031
	Natural variant	4482	1	I → V. Ref.51		VAR_067281
	Natural variant	4484	1	T → M. Corresponds to variant rs12713450 [ dbSNP | Ensembl ].		VAR_020140
Experimental info
	Mutagenesis	483	1	D → N: Impairs protein secretion. Ref.46
	Mutagenesis	483	1	D → Q: Does not affect protein secretion. Ref.46
	Mutagenesis	490	1	R → A: Impairs protein secretion. Ref.46
	Mutagenesis	490	1	R → K: Does not affect protein secretion. Ref.46
	Sequence conflict	11 – 13	3	Missing in AAB60718. Ref.5
	Sequence conflict	11 – 13	3	Missing in CAA28420. Ref.5
	Sequence conflict	329	1	L → V in AAA35549. Ref.3
	Sequence conflict	645	1	L → I in AAA35549. Ref.3
	Sequence conflict	704	1	L → P in AAB04636. Ref.4
	Sequence conflict	792 – 809	18	LQLLG…TLQGI → SSSWKAASHGCPHSAGD in AAA51759. Ref.12
	Sequence conflict	793	1	Q → R in AAB04636. Ref.4
	Sequence conflict	893	1	D → K AA sequence Ref.13
	Sequence conflict	919	1	A → P in AAA35549. Ref.3
	Sequence conflict	1109	1	H → D in CAA28420. Ref.5
	Sequence conflict	1180	1	T → R in AAA51752. Ref.8
	Sequence conflict	1271	1	F → S in AAB04636. Ref.4
	Sequence conflict	1418	1	F → S in CAA28420. Ref.5
	Sequence conflict	1445	1	N → I in AAA51752. Ref.8
	Sequence conflict	1535	1	G → E in AAA51752. Ref.8
	Sequence conflict	1867	1	R → G in AAB04636. Ref.4
	Sequence conflict	2098	1	N → K in CAA28420. Ref.5
	Sequence conflict	2218	1	I → T in AAB04636. Ref.4
	Sequence conflict	2221	1	N → I in CAA28420. Ref.5
	Sequence conflict	2324 – 2326	3	LIG → PYW in AAA51741. Ref.16
	Sequence conflict	2353	1	Q → H in AAA51741. Ref.16
	Sequence conflict	2540	1	G → S in CAA28420. Ref.5
	Sequence conflict	2718 – 2737	20	Missing in AAA51758. Ref.15
	Sequence conflict	2933	1	C → S in AAB04636. Ref.4
	Sequence conflict	3114	1	H → L AA sequence Ref.13
	Sequence conflict	3131	1	T → R AA sequence Ref.13
	Sequence conflict	3134	1	E → P AA sequence Ref.13
	Sequence conflict	3137	1	L → R AA sequence Ref.13
	Sequence conflict	3239	1	H → Q in CAA28420. Ref.5
	Sequence conflict	3286	1	L → I in AAB04636. Ref.4
	Sequence conflict	3291	1	R → L in AAA51758. Ref.15
	Sequence conflict	3337	1	I → N in AAA51758. Ref.15
	Sequence conflict	3431	1	A → P in AAB04636. Ref.4
	Sequence conflict	3728	1	D → N in AAA51742. Ref.24
	Sequence conflict	3782	1	N → T in AAB04636. Ref.4
	Sequence conflict	3824	1	Q → R in CAA28420. Ref.5
	Sequence conflict	3824	1	Q → R in AAA51750. Ref.23
	Sequence conflict	3876	1	V → A in AAA35549. Ref.3
	Sequence conflict	3876	1	V → A in AAA51742. Ref.24
	Sequence conflict	3911	1	T → Y AA sequence Ref.10
	Sequence conflict	3983	1	F → S in AAA51742. Ref.24
	Sequence conflict	4002	1	A → P in AAA51742. Ref.24
	Sequence conflict	4110 – 4111	2	NN → DH in AAA35549. Ref.3
	Sequence conflict	4110 – 4111	2	NN → DH in AAA51742. Ref.24
	Sequence conflict	4122	1	Q → E in AAA35549. Ref.3
	Sequence conflict	4122	1	Q → E in AAA51742. Ref.24
	Sequence conflict	4128	1	V → E in AAA35549. Ref.3
	Sequence conflict	4128	1	V → E in AAA51742. Ref.24
	Sequence conflict	4133	1	A → G in AAA35549. Ref.3
	Sequence conflict	4133	1	A → G in AAA51742. Ref.24
	Sequence conflict	4188	1	H → K in AAB04636. Ref.4
	Sequence conflict	4217 – 4218	2	CT → FP in AAA35548. Ref.26
	Sequence conflict	4221	1	I → M in AAB04636. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P04114 [UniParc]. Last modified July 13, 2010. Version 2. Checksum: 6800F94BF6ADF698	FASTA	4,563	515,605
	10 20 30 40 50 60 MDPPRPALLA LLALPALLLL LLAGARAEEE MLENVSLVCP KDATRFKHLR KYTYNYEAES 70 80 90 100 110 120 SSGVPGTADS RSATRINCKV ELEVPQLCSF ILKTSQCTLK EVYGFNPEGK ALLKKTKNSE 130 140 150 160 170 180 EFAAAMSRYE LKLAIPEGKQ VFLYPEKDEP TYILNIKRGI ISALLVPPET EEAKQVLFLD 190 200 210 220 230 240 TVYGNCSTHF TVKTRKGNVA TEISTERDLG QCDRFKPIRT GISPLALIKG MTRPLSTLIS 250 260 270 280 290 300 SSQSCQYTLD AKRKHVAEAI CKEQHLFLPF SYKNKYGMVA QVTQTLKLED TPKINSRFFG 310 320 330 340 350 360 EGTKKMGLAF ESTKSTSPPK QAEAVLKTLQ ELKKLTISEQ NIQRANLFNK LVTELRGLSD 370 380 390 400 410 420 EAVTSLLPQL IEVSSPITLQ ALVQCGQPQC STHILQWLKR VHANPLLIDV VTYLVALIPE 430 440 450 460 470 480 PSAQQLREIF NMARDQRSRA TLYALSHAVN NYHKTNPTGT QELLDIANYL MEQIQDDCTG 490 500 510 520 530 540 DEDYTYLILR VIGNMGQTME QLTPELKSSI LKCVQSTKPS LMIQKAAIQA LRKMEPKDKD 550 560 570 580 590 600 QEVLLQTFLD DASPGDKRLA AYLMLMRSPS QADINKIVQI LPWEQNEQVK NFVASHIANI 610 620 630 640 650 660 LNSEELDIQD LKKLVKEALK ESQLPTVMDF RKFSRNYQLY KSVSLPSLDP ASAKIEGNLI 670 680 690 700 710 720 FDPNNYLPKE SMLKTTLTAF GFASADLIEI GLEGKGFEPT LEALFGKQGF FPDSVNKALY 730 740 750 760 770 780 WVNGQVPDGV SKVLVDHFGY TKDDKHEQDM VNGIMLSVEK LIKDLKSKEV PEARAYLRIL 790 800 810 820 830 840 GEELGFASLH DLQLLGKLLL MGARTLQGIP QMIGEVIRKG SKNDFFLHYI FMENAFELPT 850 860 870 880 890 900 GAGLQLQISS SGVIAPGAKA GVKLEVANMQ AELVAKPSVS VEFVTNMGII IPDFARSGVQ 910 920 930 940 950 960 MNTNFFHESG LEAHVALKAG KLKFIIPSPK RPVKLLSGGN TLHLVSTTKT EVIPPLIENR 970 980 990 1000 1010 1020 QSWSVCKQVF PGLNYCTSGA YSNASSTDSA SYYPLTGDTR LELELRPTGE IEQYSVSATY 1030 1040 1050 1060 1070 1080 ELQREDRALV DTLKFVTQAE GAKQTEATMT FKYNRQSMTL SSEVQIPDFD VDLGTILRVN 1090 1100 1110 1120 1130 1140 DESTEGKTSY RLTLDIQNKK ITEVALMGHL SCDTKEERKI KGVISIPRLQ AEARSEILAH 1150 1160 1170 1180 1190 1200 WSPAKLLLQM DSSATAYGST VSKRVAWHYD EEKIEFEWNT GTNVDTKKMT SNFPVDLSDY 1210 1220 1230 1240 1250 1260 PKSLHMYANR LLDHRVPQTD MTFRHVGSKL IVAMSSWLQK ASGSLPYTQT LQDHLNSLKE 1270 1280 1290 1300 1310 1320 FNLQNMGLPD FHIPENLFLK SDGRVKYTLN KNSLKIEIPL PFGGKSSRDL KMLETVRTPA 1330 1340 1350 1360 1370 1380 LHFKSVGFHL PSREFQVPTF TIPKLYQLQV PLLGVLDLST NVYSNLYNWS ASYSGGNTST 1390 1400 1410 1420 1430 1440 DHFSLRARYH MKADSVVDLL SYNVQGSGET TYDHKNTFTL SYDGSLRHKF LDSNIKFSHV 1450 1460 1470 1480 1490 1500 EKLGNNPVSK GLLIFDASSS WGPQMSASVH LDSKKKQHLF VKEVKIDGQF RVSSFYAKGT 1510 1520 1530 1540 1550 1560 YGLSCQRDPN TGRLNGESNL RFNSSYLQGT NQITGRYEDG TLSLTSTSDL QSGIIKNTAS 1570 1580 1590 1600 1610 1620 LKYENYELTL KSDTNGKYKN FATSNKMDMT FSKQNALLRS EYQADYESLR FFSLLSGSLN 1630 1640 1650 1660 1670 1680 SHGLELNADI LGTDKINSGA HKATLRIGQD GISTSATTNL KCSLLVLENE LNAELGLSGA 1690 1700 1710 1720 1730 1740 SMKLTTNGRF REHNAKFSLD GKAALTELSL GSAYQAMILG VDSKNIFNFK VSQEGLKLSN 1750 1760 1770 1780 1790 1800 DMMGSYAEMK FDHTNSLNIA GLSLDFSSKL DNIYSSDKFY KQTVNLQLQP YSLVTTLNSD 1810 1820 1830 1840 1850 1860 LKYNALDLTN NGKLRLEPLK LHVAGNLKGA YQNNEIKHIY AISSAALSAS YKADTVAKVQ 1870 1880 1890 1900 1910 1920 GVEFSHRLNT DIAGLASAID MSTNYNSDSL HFSNVFRSVM APFTMTIDAH TNGNGKLALW 1930 1940 1950 1960 1970 1980 GEHTGQLYSK FLLKAEPLAF TFSHDYKGST SHHLVSRKSI SAALEHKVSA LLTPAEQTGT 1990 2000 2010 2020 2030 2040 WKLKTQFNNN EYSQDLDAYN TKDKIGVELT GRTLADLTLL DSPIKVPLLL SEPINIIDAL 2050 2060 2070 2080 2090 2100 EMRDAVEKPQ EFTIVAFVKY DKNQDVHSIN LPFFETLQEY FERNRQTIIV VLENVQRNLK 2110 2120 2130 2140 2150 2160 HINIDQFVRK YRAALGKLPQ QANDYLNSFN WERQVSHAKE KLTALTKKYR ITENDIQIAL 2170 2180 2190 2200 2210 2220 DDAKINFNEK LSQLQTYMIQ FDQYIKDSYD LHDLKIAIAN IIDEIIEKLK SLDEHYHIRV 2230 2240 2250 2260 2270 2280 NLVKTIHDLH LFIENIDFNK SGSSTASWIQ NVDTKYQIRI QIQEKLQQLK RHIQNIDIQH 2290 2300 2310 2320 2330 2340 LAGKLKQHIE AIDVRVLLDQ LGTTISFERI NDILEHVKHF VINLIGDFEV AEKINAFRAK 2350 2360 2370 2380 2390 2400 VHELIERYEV DQQIQVLMDK LVELAHQYKL KETIQKLSNV LQQVKIKDYF EKLVGFIDDA 2410 2420 2430 2440 2450 2460 VKKLNELSFK TFIEDVNKFL DMLIKKLKSF DYHQFVDETN DKIREVTQRL NGEIQALELP 2470 2480 2490 2500 2510 2520 QKAEALKLFL EETKATVAVY LESLQDTKIT LIINWLQEAL SSASLAHMKA KFRETLEDTR 2530 2540 2550 2560 2570 2580 DRMYQMDIQQ ELQRYLSLVG QVYSTLVTYI SDWWTLAAKN LTDFAEQYSI QDWAKRMKAL 2590 2600 2610 2620 2630 2640 VEQGFTVPEI KTILGTMPAF EVSLQALQKA TFQTPDFIVP LTDLRIPSVQ INFKDLKNIK 2650 2660 2670 2680 2690 2700 IPSRFSTPEF TILNTFHIPS FTIDFVEMKV KIIRTIDQML NSELQWPVPD IYLRDLKVED 2710 2720 2730 2740 2750 2760 IPLARITLPD FRLPEIAIPE FIIPTLNLND FQVPDLHIPE FQLPHISHTI EVPTFGKLYS 2770 2780 2790 2800 2810 2820 ILKIQSPLFT LDANADIGNG TTSANEAGIA ASITAKGESK LEVLNFDFQA NAQLSNPKIN 2830 2840 2850 2860 2870 2880 PLALKESVKF SSKYLRTEHG SEMLFFGNAI EGKSNTVASL HTEKNTLELS NGVIVKINNQ 2890 2900 2910 2920 2930 2940 LTLDSNTKYF HKLNIPKLDF SSQADLRNEI KTLLKAGHIA WTSSGKGSWK WACPRFSDEG 2950 2960 2970 2980 2990 3000 THESQISFTI EGPLTSFGLS NKINSKHLRV NQNLVYESGS LNFSKLEIQS QVDSQHVGHS 3010 3020 3030 3040 3050 3060 VLTAKGMALF GEGKAEFTGR HDAHLNGKVI GTLKNSLFFS AQPFEITAST NNEGNLKVRF 3070 3080 3090 3100 3110 3120 PLRLTGKIDF LNNYALFLSP SAQQASWQVS ARFNQYKYNQ NFSAGNNENI MEAHVGINGE 3130 3140 3150 3160 3170 3180 ANLDFLNIPL TIPEMRLPYT IITTPPLKDF SLWEKTGLKE FLKTTKQSFD LSVKAQYKKN 3190 3200 3210 3220 3230 3240 KHRHSITNPL AVLCEFISQS IKSFDRHFEK NRNNALDFVT KSYNETKIKF DKYKAEKSHD 3250 3260 3270 3280 3290 3300 ELPRTFQIPG YTVPVVNVEV SPFTIEMSAF GYVFPKAVSM PSFSILGSDV RVPSYTLILP 3310 3320 3330 3340 3350 3360 SLELPVLHVP RNLKLSLPDF KELCTISHIF IPAMGNITYD FSFKSSVITL NTNAELFNQS 3370 3380 3390 3400 3410 3420 DIVAHLLSSS SSVIDALQYK LEGTTRLTRK RGLKLATALS LSNKFVEGSH NSTVSLTTKN 3430 3440 3450 3460 3470 3480 MEVSVATTTK AQIPILRMNF KQELNGNTKS KPTVSSSMEF KYDFNSSMLY STAKGAVDHK 3490 3500 3510 3520 3530 3540 LSLESLTSYF SIESSTKGDV KGSVLSREYS GTIASEANTY LNSKSTRSSV KLQGTSKIDD 3550 3560 3570 3580 3590 3600 IWNLEVKENF AGEATLQRIY SLWEHSTKNH LQLEGLFFTN GEHTSKATLE LSPWQMSALV 3610 3620 3630 3640 3650 3660 QVHASQPSSF HDFPDLGQEV ALNANTKNQK IRWKNEVRIH SGSFQSQVEL SNDQEKAHLD 3670 3680 3690 3700 3710 3720 IAGSLEGHLR FLKNIILPVY DKSLWDFLKL DVTTSIGRRQ HLRVSTAFVY TKNPNGYSFS 3730 3740 3750 3760 3770 3780 IPVKVLADKF IIPGLKLNDL NSVLVMPTFH VPFTDLQVPS CKLDFREIQI YKKLRTSSFA 3790 3800 3810 3820 3830 3840 LNLPTLPEVK FPEVDVLTKY SQPEDSLIPF FEITVPESQL TVSQFTLPKS VSDGIAALDL 3850 3860 3870 3880 3890 3900 NAVANKIADF ELPTIIVPEQ TIEIPSIKFS VPAGIVIPSF QALTARFEVD SPVYNATWSA 3910 3920 3930 3940 3950 3960 SLKNKADYVE TVLDSTCSST VQFLEYELNV LGTHKIEDGT LASKTKGTFA HRDFSAEYEE 3970 3980 3990 4000 4010 4020 DGKYEGLQEW EGKAHLNIKS PAFTDLHLRY QKDKKGISTS AASPAVGTVG MDMDEDDDFS 4030 4040 4050 4060 4070 4080 KWNFYYSPQS SPDKKLTIFK TELRVRESDE ETQIKVNWEE EAASGLLTSL KDNVPKATGV 4090 4100 4110 4120 4130 4140 LYDYVNKYHW EHTGLTLREV SSKLRRNLQN NAEWVYQGAI RQIDDIDVRF QKAASGTTGT 4150 4160 4170 4180 4190 4200 YQEWKDKAQN LYQELLTQEG QASFQGLKDN VFDGLVRVTQ EFHMKVKHLI DSLIDFLNFP 4210 4220 4230 4240 4250 4260 RFQFPGKPGI YTREELCTMF IREVGTVLSQ VYSKVHNGSE ILFSYFQDLV ITLPFELRKH 4270 4280 4290 4300 4310 4320 KLIDVISMYR ELLKDLSKEA QEVFKAIQSL KTTEVLRNLQ DLLQFIFQLI EDNIKQLKEM 4330 4340 4350 4360 4370 4380 KFTYLINYIQ DEINTIFSDY IPYVFKLLKE NLCLNLHKFN EFIQNELQEA SQELQQIHQY 4390 4400 4410 4420 4430 4440 IMALREEYFD PSIVGWTVKY YELEEKIVSL IKNLLVALKD FHSEYIVSAS NFTSQLSSQV 4450 4460 4470 4480 4490 4500 EQFLHRNIQE YLSILTDPDG KGKEKIAELS ATAQEIIKSQ AIATKKIISD YHQQFRYKLQ 4510 4520 4530 4540 4550 4560 DFSDQLSDYY EKFIAESKRL IDLSIQNYHT FLIYITELLK KLQSTTVMNP YMKLAPGELT IIL

References

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[1]	"Complete cDNA and derived protein sequence of human apolipoprotein B-100." 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. Nucleic Acids Res. 14:7501-7503(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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.
[2]	"DNA sequence of the human apolipoprotein B gene." 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 6:363-372(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
[3]	"The complete cDNA and amino acid sequence of human apolipoprotein B-100." Chen S.-H., Yang C.-Y., Chen P.-F., Setzer D., Tanimura M., Li W.-H., Gotto A.M. Jr., Chan L. J. Biol. Chem. 261:12918-12921(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-98; VAL-618; CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
[4]	"Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence." Law S.W., Grant S.M., Higuchi K., Hospattankar A.V., Lackner K.J., Lee N., Brewer H.B. Jr. Proc. Natl. Acad. Sci. U.S.A. 83:8142-8146(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CYS-1422; ASN-2037; VAL-2313; HIS-3319; LYS-3427; GLU-3432; LEU-3949; LYS-4181 AND ASN-4338.
[5]	"The complete sequence and structural analysis of human apolipoprotein B-100: relationship between apoB-100 and apoB-48 forms." Cladaras C., Hadzopoulou-Cladaras M., Nolte R.T., Atkinson D., Zannis V.I. EMBO J. 5:3495-3507(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40, VARIANTS VAL-618; CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
[6]	SeattleSNPs variation discovery resource Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-1422; VAL-2313 AND ASN-4338.
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[8]	"Analysis of cDNA clones encoding the entire B-26 region of human apolipoprotein B." 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. Proc. Natl. Acad. Sci. U.S.A. 83:5678-5682(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1670, VARIANTS ILE-98; CYS-1422 AND ASP-1670.
[9]	"Isolation of a cDNA clone encoding the amino-terminal region of human apolipoprotein B." Protter A.A., Hardman D.A., Schilling J.W., Miller J., Appleby V., Chen G.C., Kirsher S.W., McEnroe G., Kane J.P. Proc. Natl. Acad. Sci. U.S.A. 83:1467-1471(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-291.
[10]	"Isolation and characterization of sulfhydryl and disulfide peptides of human apolipoprotein B-100." Yang C.Y., Kim T.W., Weng S.A., Lee B.R., Yang M.L., Gotto A.M. Jr. Proc. Natl. Acad. Sci. U.S.A. 87:5523-5527(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, VARIANT ILE-98.
[11]	"Human apolipoprotein B-100: cloning, analysis of liver mRNA, and assignment of the gene to chromosome 2." Law S.W., Lackner K.J., Hospattankar A.V., Anchors J.M., Sakaguchi A.Y., Naylor S.L., Brewer H.B. Jr. Proc. Natl. Acad. Sci. U.S.A. 82:8340-8344(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 485-1044. Tissue: Liver.
[12]	"A partial cDNA clone for human apolipoprotein B." Deeb S.S., Motulsky A.G., Albers J.J. Proc. Natl. Acad. Sci. U.S.A. 82:4983-4986(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 709-906.
[13]	"Human apolipoprotein B: partial amino acid sequence." LeBoeuf R.C., Miller C., Shively J.E., Schumaker V.N., Balla M.A., Lusis A.J. FEBS Lett. 170:105-108(1984) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 873-896 AND 3113-3137.
[14]	"Hypobetalipoproteinemia due to an apolipoprotein B gene exon 21 deletion derived by Alu-Alu recombination." Huang L.S., Ripps M.E., Korman S.H., Deckelbaum R.J., Breslow J.L. J. Biol. Chem. 264:11394-11400(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1042-1232.
[15]	"Analysis of the human apolipoprotein B gene; complete structure of the B-74 region." Carlsson P., Darnfors C., Olofsson S.O., Bjursell G. Gene 49:29-51(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1282-4503, VARIANTS CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432; THR-3732 AND ASN-4338.
[16]	"Structural comparison of human apolipoproteins B-48 and B-100." 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. Biochemistry 26:5478-5486(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1671-2398, VARIANT VAL-2313.
[17]	"Molecular cloning of human apolipoprotein B cDNA." Carlsson P., Olofsson S.O., Bondjers G., Darnfors C., Wiklund O., Bjursell G. Nucleic Acids Res. 13:8813-8826(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1937-2018 AND 3811-4334.
[18]	"A novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine." Powell L.M., Wallis S.C., Pease R.J., Edwards Y.H., Knott T.J., Scott J. Cell 50:831-840(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2115-2179. Tissue: Small intestine.
[19]	"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." Higuchi K., Hospattankar A.V., Law S.W., Meglin N., Cortright J., Brewer H.B. Jr. Proc. Natl. Acad. Sci. U.S.A. 85:1772-1776(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2127-2179.
[20]	"Carboxyl terminal analysis of human B-48 protein confirms the novel mechanism proposed for chain termination." Hardman D.A., Protter A.A., Schilling J.W., Kane J.P. Biochem. Biophys. Res. Commun. 149:1214-1219(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2129-2235.
[21]	"Identification of a novel in-frame translational stop codon in human intestine apoB mRNA." Hospattankar A.V., Higuchi K., Law S.W., Meglin N., Brewer H.B. Jr. Biochem. Biophys. Res. Commun. 148:279-285(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2169-2179.
[22]	"Human apolipoprotein B: identification of cDNA clones and characterization of mRNA." 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. Nucleic Acids Res. 13:6937-6953(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3056-3159.
[23]	"Human apolipoprotein B: structure of carboxyl-terminal domains, sites of gene expression, and chromosomal localization." 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. Science 230:37-43(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3109-4563, VARIANTS HIS-3319; LYS-3427; GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
[24]	"Molecular cloning and expression of partial cDNAs and deduced amino acid sequence of a carboxyl-terminal fragment of human apolipoprotein B-100." 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. Proc. Natl. Acad. Sci. U.S.A. 82:7265-7269(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3728-4563, VARIANT ASN-4338.
[25]	"Molecular cloning of human LDL apolipoprotein B cDNA. Evidence for more than one gene per haploid genome." Shoulders C.C., Myant N.B., Sidoli A., Rodriguez J.C., Cortese C., Baralle F.E., Cortese R. Atherosclerosis 58:277-289(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3846-4298, VARIANTS LEU-3949; PHE-3964 AND LYS-4181. Tissue: Liver.
[26]	"Isolation, expression and characterization of a human apolipoprotein B 100-specific cDNA clone." Pfitzner R., Wagener R., Stoffel W. Biol. Chem. Hoppe-Seyler 367:1077-1083(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4217-4563.
[27]	"Apolipoprotein B-48 is the product of a messenger RNA with an organ-specific in-frame stop codon." 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. Science 238:363-366(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION OF APO-B48.
[28]	"Complete protein sequence and identification of structural domains of human apolipoprotein B." 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. Nature 323:734-738(1986) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAINS.
[29]	"Sequence, structure, receptor-binding domains and internal repeats of human apolipoprotein B-100." 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. Nature 323:738-742(1986) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAINS.
[30]	"Apolipoprotein B is a calcium binding protein." Dashti N., Lee D.M., Mok T. Biochem. Biophys. Res. Commun. 137:493-499(1986) [PubMed] [Europe PMC] [Abstract] Cited for: CALCIUM-BINDING.
[31]	"Palmitoylation of apolipoprotein B is required for proper intracellular sorting and transport of cholesteroyl esters and triglycerides." Zhao Y., McCabe J.B., Vance J., Berthiaume L.G. Mol. Biol. Cell 11:721-734(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-1112.
[32]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3358, MASS SPECTROMETRY. Tissue: Plasma.
[33]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1523; ASN-2982; ASN-3465 AND ASN-3895, MASS SPECTROMETRY. Tissue: Plasma.
[34]	"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection." Leong W.F., Chow V.T. Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, MASS SPECTROMETRY.
[35]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: 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, MASS SPECTROMETRY. Tissue: Liver.
[36]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2004, MASS SPECTROMETRY.
[37]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]	"Proprotein convertase subtilisin/kexin type 9 interacts with apolipoprotein B and prevents its intracellular degradation, irrespective of the low-density lipoprotein receptor." Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B. Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PCSK9.
[39]	"Detection by denaturing gradient gel electrophoresis of a new polymorphism in the apolipoprotein B gene." Navajas M., Laurent A.-M., Moreel J.-F., Ragab A., Cambou J.-P., Cunny G., Cambien F., Roizes G. Hum. Genet. 86:91-93(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ASN-4338.
[40]	"Association between a specific apolipoprotein B mutation and familial defective apolipoprotein B-100." Soria L.F., Ludwig E.H., Clarke H.R.G., Vega G.L., Grundy S.M., McCarthy B.J. Proc. Natl. Acad. Sci. U.S.A. 86:587-591(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FDB GLN-3527.
[41]	"Sequence polymorphism in the human apoB gene at position 8344." Huang L.-S., Gavish D., Breslow J.L. Nucleic Acids Res. 18:5922-5922(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LEU-2739.
[42]	"Familial ligand-defective apolipoprotein B. Identification of a new mutation that decreases LDL receptor binding affinity." 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. J. Clin. Invest. 95:1225-1234(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FDB CYS-3558.
[43]	"Detection of new variants in the apolipoprotein B (Apo B) gene by PCR-SSCP." Poirier O., Ricard S., Behague I., Souriau C., Evans A.E., Arveiler D., Marques-Vidal P., Luc G., Roizes G., Cambien F. Hum. Mutat. 8:282-285(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LEU-1437; SER-1914; LYS-2566; THR-3121; ALA-3945; MET-4128 AND THR-4481.
[44]	"Familial ligand-defective apolipoprotein B-100: simultaneous detection of the Arg3500-->Gln and Arg3531-->Cys mutations in a French population." Rabes J.P., Varret M., Saint-Jore B., Erlich D., Jondeau G., Krempf M., Giraudet P., Junien C., Boileau C. Hum. Mutat. 10:160-163(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FDB GLN-3527 AND CYS-3558.
[45]	"Screening for mutations of the apolipoprotein B gene causing hypocholesterolemia." Leren T.P., Bakken K.S., Hoel V., Hjermann I., Berg K. Hum. Genet. 102:44-49(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SER-1914; ARG-1923; LEU-2739; HIS-3319; LYS-3427; GLU-3432 AND ILE-3921.
[46]	"A novel nontruncating APOB gene mutation, R463W, causes familial hypobetalipoproteinemia." Burnett J.R., Shan J., Miskie B.A., Whitfield A.J., Yuan J., Tran K., McKnight C.J., Hegele R.A., Yao Z. J. Biol. Chem. 278:13442-13452(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FHBL1 TRP-490, VARIANT ILE-98, CHARACTERIZATION OF VARIANT TRP-490, MUTAGENESIS OF ASP-483 AND ARG-490.
[47]	"Hypobetalipoproteinemia with an apparently recessive inheritance due to a 'de novo' mutation of apolipoprotein B." Lancellotti S., Di Leo E., Penacchioni J.Y., Balli F., Viola L., Bertolini S., Calandra S., Tarugi P. Biochim. Biophys. Acta 1688:61-67(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HIS-1128.
[48]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-2564.
[49]	"Molecular basis of autosomal dominant hypercholesterolemia: assessment in a large cohort of hypercholesterolemic children." 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. Circulation 123:1167-1173(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FDB GLN-3527.
[50]	"Quantitative detection of single amino acid polymorphisms by targeted proteomics." 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. J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLU-1218; ASP-1670; ASN-2037; CYS-2564 AND LYS-2566, MASS SPECTROMETRY.
[51]	"Genetic variation in APOB, PCSK9, and ANGPTL3 in carriers of pathogenic autosomal dominant hypercholesterolemic mutations with unexpected low LDL-Cl Levels." Huijgen R., Sjouke B., Vis K., de Randamie J.S., Defesche J.C., Kastelein J.J., Hovingh G.K., Fouchier S.W. Hum. Mutat. 33:448-455(2012) [PubMed] [Europe PMC] [Abstract] Cited for: 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.
+	Additional computationally mapped references.

Web resources

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Apolipoprotein B entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04506 mRNA. Translation: CAA28191.1. M19828 , M19808, M19809, M19810, M19811, M19812, M19813, M19815, M19816, M19818, M19820, M19821, M19823, M19824, M19825, M19827 Genomic DNA. Translation: AAB00481.1. J02610 mRNA. Translation: AAA35549.1. M14162 mRNA. Translation: AAB04636.1. M15053 Genomic DNA. Translation: AAB60718.1. X04714 mRNA. Translation: CAA28420.1. AY324608 Genomic DNA. Translation: AAP72970.1. AC010872 Genomic DNA. Translation: AAX88848.1. AC115619 Genomic DNA. Translation: AAX93246.1. M14081 mRNA. Translation: AAA51752.1. Frameshift. M12681 mRNA. Translation: AAA51753.1. M12480 mRNA. Translation: AAA51751.1. K03175 mRNA. Translation: AAA51759.1. M15421 mRNA. Translation: AAA51758.1. M17367 mRNA. Translation: AAA51741.1. M31030 mRNA. Translation: AAA51756.1. X03325 mRNA. Translation: CAA27044.1. X03326 mRNA. Translation: CAA27045.1. M17779 mRNA. Translation: AAA51755.1. M19734 mRNA. Translation: AAA35544.1. M18471 mRNA. Translation: AAA35541.1. X03045 mRNA. Translation: CAA26850.1. M10374 mRNA. Translation: AAA51750.1. M12413 mRNA. Translation: AAA51742.1. M36676 mRNA. Translation: AAA35548.1.
IPI	IPI00022229.
PIR	LPHUB. A27850.
RefSeq	NP_000375.2. NM_000384.2.
UniGene	Hs.120759.
3D structure databases
ProteinModelPortal	P04114.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-44767N.
IntAct	P04114. 4 interactions.
PTM databases
GlycoSuiteDB	P04114.
PhosphoSite	P04114.
Polymorphism databases
DMDM	300669605.
Proteomic databases
PaxDb	P04114.
PeptideAtlas	P04114.
PRIDE	P04114.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000233242; ENSP00000233242; ENSG00000084674.
GeneID	338.
KEGG	hsa:338.
Organism-specific databases
CTD	338.
GeneCards	GC02M021135.
H-InvDB	HIX0024005.
HGNC	HGNC:603. APOB.
HPA	CAB016070.
MIM	107730. gene+phenotype. 144010. phenotype.
neXtProt	NX_P04114.
Orphanet	14. Abetalipoproteinemia. 181434. Benign familial hypobetalipoproteinemia. 406. Familial hypercholesterolemia.
PharmGKB	PA50.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG290405.
HOVERGEN	HBG050546.
InParanoid	P04114.
KO	K14462.
OMA	HIPEFQL.
OrthoDB	EOG47WNMR.
PhylomeDB	P04114.
Enzyme and pathway databases
Pathway_Interaction_DB	amb2_neutrophils_pathway. amb2 Integrin signaling. hnf3apathway. FOXA1 transcription factor network.
Reactome	REACT_111217. Metabolism. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P04114.
Bgee	P04114.
Genevestigator	P04114.
GermOnline	ENSG00000084674. Homo sapiens.
Family and domain databases
Gene3D	1.25.10.20. 1 hit. 2.20.50.20. 2 hits. 2.20.80.10. 1 hit. 2.30.230.10. 1 hit.
InterPro	IPR022176. ApoB100_C. IPR015819. Lipid_transp_b-sht_shell. IPR001747. Lipid_transpt_N. IPR009454. Lipid_transpt_open_b-sht. IPR015816. Vitellinogen_b-sht_N. IPR015255. Vitellinogen_open_b-sht. IPR015817. Vitellinogen_open_b-sht_sub1. IPR015818. Vitellinogen_open_b-sht_sub2. IPR011030. Vitellinogen_superhlx. [Graphical view]
Pfam	PF12491. ApoB100_C. 1 hit. PF06448. DUF1081. 1 hit. PF09172. DUF1943. 1 hit. PF01347. Vitellogenin_N. 1 hit. [Graphical view]
SMART	SM00638. LPD_N. 1 hit. [Graphical view]
SUPFAM	SSF56968. Lipid_transp_b-sht_shell. 2 hits. SSF48431. LV_superhelical. 1 hit.
PROSITE	PS51211. VITELLOGENIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P04114.
ChEMBL	CHEMBL4549.
ChiTaRS	APOB. human.
DrugBank	DB01076. Atorvastatin.
GenomeRNAi	338.
NextBio	1399.
SOURCE	Search...

Entry information

Entry name

APOB_HUMAN

Accession

Primary (citable) accession number: P04114
Secondary accession number(s): O00502 , P78479, P78480, P78481, Q13779, Q13785, Q13786, Q13787, Q13788, Q4ZG63, Q53QC8, Q7Z600, Q9UMN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	July 13, 2010
Last modified:	May 1, 2013
This is version 163 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.