Reviewed, UniProtKB/Swiss-Prot P04114 (APOB_HUMAN)

Names and origin

Protein names

Recommended name:
    Apolipoprotein B-100
      Short name=Apo B-100
Cleaved into the following chain:
    1- Recommended name:
            Apolipoprotein B-48
                Short name=Apo B-48

Gene names

Name:

APOB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
Subcellular location	Secreted.
Post-translational modification	Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle. Ref.30
Involvement in disease	Defects in APOB are a cause of familial hypobetalipoproteinemia (FHBL) [MIM:107730]. FHBL is a genetically heterogeneous autosomal co-dominant disorder, associated with reduced plasma concentrations of apoB, LDL and VLDL. Heterozygotes for FHBL are usually asymptomatic with LDL cholesterol and apoB-100 concentrations less than 50% of those in normal plasma. Homozygotes have extremely low plasma LDL cholesterol and apoB-100 concentrations, and clinical presentation may vary from no symptoms to severe gastrointestinal and neurological dysfunction similar to abetalipoproteinemia [MIM:200100]. Ref.43 Defects in APOB are a cause of familial ligand-defective apolipoprotein B-100 (FDB) [MIM:144010]. FDB is a 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. Ref.37 Ref.39 Ref.41 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 Transport
Cellular component	Chylomicron LDL Secreted VLDL
Coding sequence diversity	Polymorphism RNA editing
Disease	Atherosclerosis Disease mutation
Domain	Signal
Ligand	Heparin-binding
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cholesterol homeostasis Ref.37 Inferred from mutant phenotype. Source: UniProtKB cholesterol metabolic process Ref.37 Inferred from mutant phenotype. Source: UniProtKB cholesterol transport Ref.37 Inferred from mutant phenotype. Source: UniProtKB low-density lipoprotein particle clearance Ref.37 Inferred from mutant phenotype. Source: UniProtKB low-density lipoprotein particle remodeling Inferred from mutant phenotype. Source: UniProtKB positive regulation of cholesterol storage Inferred from direct assay. Source: UniProtKB positive regulation of foam cell differentiation Inferred from direct assay. Source: UniProtKB very-low-density lipoprotein particle assembly Inferred by curator. Source: UniProtKB
Cellular component	chylomicron remnant Traceable author statement. Source: UniProtKB clathrin-coated endocytic vesicle membrane Inferred from Experiment. Source: Reactome endoplasmic reticulum lumen Inferred from Experiment. Source: Reactome endosome lumen Inferred from Experiment. Source: Reactome endosome membrane Inferred from Experiment. Source: Reactome intermediate-density lipoprotein particle Inferred from direct assay. Source: UniProtKB low-density lipoprotein particle Inferred from direct assay. Source: UniProtKB mature chylomicron Inferred from direct assay. Source: UniProtKB microsome Traceable author statement. Source: ProtInc plasma membrane Inferred from Experiment. Source: Reactome very-low-density lipoprotein particle Inferred from direct assay. Source: UniProtKB
Molecular function	cholesterol transporter activity Inferred from mutant phenotype. Source: UniProtKB enzyme binding Inferred from physical interaction. Source: UniProtKB heparin binding Inferred from direct assay. Source: UniProtKB low-density lipoprotein receptor binding Ref.37 Inferred from mutant phenotype. Source: UniProtKB phospholipid binding Inferred from direct assay. Source: UniProtKB protein heterodimerization activity Inferred from physical interaction. Source: UniProtKB
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	928	1	Phosphoserine Ref.34
	Modified residue	4507	1	Phosphoserine Ref.33
	Lipidation	1112	1	S-palmitoyl cysteine Ref.30
	Glycosylation	34	1	N-linked (GlcNAc...) Potential
	Glycosylation	185	1	N-linked (GlcNAc...)
	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.32
	Glycosylation	2239	1	N-linked (GlcNAc...)
	Glycosylation	2560	1	N-linked (GlcNAc...) Potential
	Glycosylation	2779	1	N-linked (GlcNAc...)
	Glycosylation	2982	1	N-linked (GlcNAc...) Ref.32
	Glycosylation	3101	1	N-linked (GlcNAc...)
	Glycosylation	3224	1	N-linked (GlcNAc...)
	Glycosylation	3336	1	N-linked (GlcNAc...) Potential
	Glycosylation	3358	1	N-linked (GlcNAc...) Ref.31
	Glycosylation	3411	1	N-linked (GlcNAc...)
	Glycosylation	3465	1	N-linked (GlcNAc...) Ref.32
	Glycosylation	3895	1	N-linked (GlcNAc...) Ref.32
	Glycosylation	4237	1	N-linked (GlcNAc...) Potential
	Glycosylation	4431	1	N-linked (GlcNAc...) Potential
	Disulfide bond	39 ↔ 88		Ref.9
	Disulfide bond	78 ↔ 97		Ref.9
	Disulfide bond	186 ↔ 212		Ref.9
	Disulfide bond	245 ↔ 261		Ref.9
	Disulfide bond	385 ↔ 390		Ref.9
	Disulfide bond	478 ↔ 513		Ref.9
	Disulfide bond	966 ↔ 976		Ref.9
	Disulfide bond	3194 ↔ 3324		Ref.9
Natural variations
	Natural variant	98	1	T → I: dbSNP rs1367117. Ref.43 Ref.9 Ref.3 Ref.7		VAR_016184
	Natural variant	103	1	Y → H: dbSNP rs9282603.		VAR_022036
	Natural variant	145	1	P → S: dbSNP rs6752026.		VAR_022037
	Natural variant	194	1	T → M: dbSNP rs13306198.		VAR_056737
	Natural variant	273	1	N → K: dbSNP rs1126419. Ref.3 Ref.7 Ref.2 Ref.4 Ref.5 Ref.6 Ref.8		VAR_019827
	Natural variant	408	1	I → T: dbSNP rs12714225.		VAR_029341
	Natural variant	490	1	R → W in FHBL; reduced protein secretion. Ref.43		VAR_022610
	Natural variant	554	1	P → L: dbSNP rs12714214.		VAR_020135
	Natural variant	618	1	A → V: dbSNP rs679899. Ref.3 Ref.5		VAR_019828
	Natural variant	730	1	V → I: dbSNP rs12691202.		VAR_020136
	Natural variant	733	1	V → I: dbSNP rs1800476.		VAR_016185
	Natural variant	741	1	T → N: dbSNP rs12714192.		VAR_020137
	Natural variant	877	1	P → L: dbSNP rs12714097.		VAR_029342
	Natural variant	955	1	P → S: dbSNP rs13306206.		VAR_056738
	Natural variant	1086	1	G → S: dbSNP rs12720801.		VAR_029343
	Natural variant	1113	1	D → H: dbSNP rs12713844.		VAR_029344
	Natural variant	1128	1	R → H: dbSNP rs12713843. Ref.44		VAR_022611
	Natural variant	1218	1	E → Q: dbSNP rs1041956. Ref.3 Ref.7 Ref.2 Ref.4 Ref.5 Ref.6 Ref.13		VAR_019829
	Natural variant	1388	1	R → H: dbSNP rs13306187.		VAR_029345
	Natural variant	1437	1	F → L: dbSNP rs1801697. Ref.40		VAR_005016
	Natural variant	1914	1	N → S: dbSNP rs1801699. Ref.40 Ref.42		VAR_005017
	Natural variant	1923	1	H → R: dbSNP rs533617. Ref.42		VAR_005018
	Natural variant	2092	1	V → L: dbSNP rs1041960. Ref.3 Ref.2 Ref.4 Ref.5 Ref.6 Ref.14 Ref.15		VAR_019830
	Natural variant	2299	1	D → H: dbSNP rs12713681.		VAR_029346
	Natural variant	2365	1	T → A: dbSNP rs1041971. Ref.3 Ref.2 Ref.4 Ref.5 Ref.6 Ref.14 Ref.15		VAR_019831
	Natural variant	2456	1	A → D: dbSNP rs12713675.		VAR_020138
	Natural variant	2564	1	F → C in a colorectal cancer sample; somatic mutation. Ref.45		VAR_035795
	Natural variant	2566	1	E → K: dbSNP rs1801696. Ref.40		VAR_005019
	Natural variant	2680	1	Q → L: dbSNP rs1042013. Ref.3 Ref.2 Ref.4 Ref.5 Ref.6 Ref.14		VAR_019832
	Natural variant	2739	1	P → L: dbSNP rs676210. Ref.42 Ref.38		VAR_005020
	Natural variant	2785	1	N → H: dbSNP rs2163204.		VAR_022038
	Natural variant	3121	1	A → T: dbSNP rs1801694. Ref.40		VAR_005021
	Natural variant	3182	1	H → N: dbSNP rs12720848.		VAR_029347
	Natural variant	3279	1	S → G: dbSNP rs12720854.		VAR_029348
	Natural variant	3294	1	S → P: dbSNP rs12720855.		VAR_020139
	Natural variant	3319	1	H → D Ref.6 Ref.42		VAR_005022
	Natural variant	3427	1	K → T Ref.6 Ref.42		VAR_005023
	Natural variant	3432	1	E → Q: dbSNP rs1042023. Ref.6 Ref.42		VAR_005024
	Natural variant	3527	1	R → Q in FDB. dbSNP rs5742904. Ref.37 Ref.41		VAR_005025
	Natural variant	3558	1	R → C in FDB. dbSNP rs12713559. Ref.39 Ref.41		VAR_005026
	Natural variant	3638	1	R → Q: dbSNP rs1801701.		VAR_016186
	Natural variant	3732	1	T → I: dbSNP rs1042025. Ref.3 Ref.2 Ref.4 Ref.6 Ref.23		VAR_019833
	Natural variant	3801	1	S → T: dbSNP rs12713540.		VAR_029349
	Natural variant	3921	1	V → I Ref.42		VAR_005027
	Natural variant	3945	1	T → A: dbSNP rs1801698. Ref.40		VAR_005028
	Natural variant	3949	1	L → F: dbSNP rs1042027. Ref.3 Ref.2 Ref.6 Ref.14 Ref.23 Ref.16		VAR_019834
	Natural variant	3964	1	F → Y: dbSNP rs1126468. Ref.3 Ref.2 Ref.4 Ref.6 Ref.14 Ref.23 Ref.16		VAR_019835
	Natural variant	4128	1	V → M: dbSNP rs1801703. Ref.40		VAR_005029
	Natural variant	4181	1	K → E: dbSNP rs1042031. Ref.3 Ref.2 Ref.6 Ref.14 Ref.23 Ref.16		VAR_016187
	Natural variant	4270	1	R → T: dbSNP rs1801702.		VAR_016188
	Natural variant	4338	1	N → S: dbSNP rs1042034. Ref.25 Ref.36		VAR_005030
	Natural variant	4394	1	V → A: dbSNP rs12720843.		VAR_029350
	Natural variant	4481	1	A → T: dbSNP rs1801695. Ref.40		VAR_005031
	Natural variant	4484	1	T → M: dbSNP rs12713450.		VAR_020140
Experimental info
	Mutagenesis	483	1	D → N: Impairs protein secretion. Ref.43
	Mutagenesis	483	1	D → Q: Does not affect protein secretion. Ref.43
	Mutagenesis	490	1	R → A: Impairs protein secretion. Ref.43
	Mutagenesis	490	1	R → K: Does not affect protein secretion. Ref.43
	Sequence conflict	11 – 13	3	Missing Ref.5
	Sequence conflict	329	1	L → V Ref.3
	Sequence conflict	645	1	L → I Ref.3
	Sequence conflict	704	1	L → P Ref.4
	Sequence conflict	792 – 809	18	LQLLG…TLQGI → SSSWKAASHGCPHSAGD Ref.11
	Sequence conflict	793	1	Q → R Ref.4
	Sequence conflict	893	1	D → K AA sequence Ref.12
	Sequence conflict	919	1	A → P Ref.3
	Sequence conflict	1109	1	H → D Ref.5
	Sequence conflict	1180	1	T → R Ref.7
	Sequence conflict	1271	1	F → S Ref.4
	Sequence conflict	1418	1	F → S Ref.5
	Sequence conflict	1445	1	N → I Ref.7
	Sequence conflict	1535	1	G → E Ref.7
	Sequence conflict	1670	1	E → D Ref.7
	Sequence conflict	1867	1	R → G Ref.4
	Sequence conflict	2037	1	I → N Ref.4
	Sequence conflict	2098	1	N → K Ref.5
	Sequence conflict	2218	1	I → T Ref.4
	Sequence conflict	2221	1	N → I Ref.5
	Sequence conflict	2324 – 2326	3	LIG → PYW Ref.15
	Sequence conflict	2353	1	Q → H Ref.15
	Sequence conflict	2540	1	G → S Ref.5
	Sequence conflict	2718 – 2737	20	Missing Ref.14
	Sequence conflict	2933	1	C → S Ref.4
	Sequence conflict	3114	1	H → L AA sequence Ref.12
	Sequence conflict	3131	1	T → R AA sequence Ref.12
	Sequence conflict	3134	1	E → P AA sequence Ref.12
	Sequence conflict	3137	1	L → R AA sequence Ref.12
	Sequence conflict	3239	1	H → Q Ref.5
	Sequence conflict	3286	1	L → I Ref.4
	Sequence conflict	3291	1	R → L Ref.14
	Sequence conflict	3337	1	I → N Ref.14
	Sequence conflict	3431	1	A → P Ref.4
	Sequence conflict	3728	1	D → N Ref.23
	Sequence conflict	3782	1	N → T Ref.4
	Sequence conflict	3824	1	Q → R Ref.5
	Sequence conflict	3824	1	Q → R Ref.22
	Sequence conflict	3876	1	V → A Ref.3
	Sequence conflict	3876	1	V → A Ref.23
	Sequence conflict	3911	1	T → Y AA sequence Ref.9
	Sequence conflict	3983	1	F → S Ref.23
	Sequence conflict	4002	1	A → P Ref.23
	Sequence conflict	4110 – 4111	2	NN → DH Ref.3
	Sequence conflict	4110 – 4111	2	NN → DH Ref.23
	Sequence conflict	4122	1	Q → E Ref.3
	Sequence conflict	4122	1	Q → E Ref.23
	Sequence conflict	4128	1	V → E Ref.3
	Sequence conflict	4128	1	V → E Ref.23
	Sequence conflict	4133	1	A → G Ref.3
	Sequence conflict	4133	1	A → G Ref.23
	Sequence conflict	4188	1	H → K Ref.4
	Sequence conflict	4217 – 4218	2	CT → FP Ref.25
	Sequence conflict	4221	1	I → M Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P04114-1 [UniParc]. Last modified November 1, 1986. Version 1. Checksum: 2AD50594D3ADD22E	FASTA	4,563	515,563
	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 SYNNKYGMVA 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 LLDHRVPETD 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 SCDGSLRHKF 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 VVENVQRNLK 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 NDVLEHVKHF VINLIGDFEV AEKINAFRAK 2350 2360 2370 2380 2390 2400 VHELIERYEV DQQIQVLMDK LVELTHQYKL 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 KIIRTIDQMQ 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 RNLKLSLPHF KELCTISHIF IPAMGNITYD FSFKSSVITL NTNAELFNQS 3370 3380 3390 3400 3410 3420 DIVAHLLSSS SSVIDALQYK LEGTTRLTRK RGLKLATALS LSNKFVEGSH NSTVSLTTKN 3430 3440 3450 3460 3470 3480 MEVSVAKTTK AEIPILRMNF 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 ITPGLKLNDL 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 LASKTKGTLA HRDFSAEYEE 3970 3980 3990 4000 4010 4020 DGKFEGLQEW 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 KFHMKVKHLI 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 DEINTIFNDY 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

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3763409] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 3652907] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-273; GLN-1218; LEU-2092; ALA-2365; LEU-2680; ILE-3732; PHE-3949; TYR-3964 AND GLU-4181.
[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: 3759943] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-98; LYS-273; VAL-618; GLN-1218; LEU-2092; ALA-2365; LEU-2680; ILE-3732; PHE-3949; TYR-3964 AND GLU-4181.
[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: 3464946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LYS-273; GLN-1218; LEU-2092; ALA-2365; LEU-2680; ILE-3732 AND TYR-3964.
[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: 3030729] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-273; VAL-618; GLN-1218; LEU-2092; ALA-2365 AND LEU-2680.
[6]	SeattleSNPs variation discovery resource Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-273; GLN-1218; LEU-2092; ALA-2365; LEU-2680; ASP-3319; THR-3427; GLN-3432; ILE-3732; PHE-3949; TYR-3964 AND GLU-4181.
[7]	"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: 3461454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1670, VARIANTS ILE-98; LYS-273 AND GLN-1218.
[8]	"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: 3513177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-291, VARIANT LYS-273.
[9]	"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: 2115173] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, VARIANT ILE-98.
[10]	"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: 3001697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 485-1044. Tissue: Liver.
[11]	"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: 3860836] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 709-906.
[12]	"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: 6373369] [Abstract] Cited for: PROTEIN SEQUENCE OF 873-896 AND 3113-3137.
[13]	"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: 2567736] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1042-1232, VARIANT GLN-1218.
[14]	"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: 2883086] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1282-4503, VARIANTS LEU-2092; ALA-2365; LEU-2680; PHE-3949; TYR-3964 AND GLU-4181.
[15]	"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: 3676265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1671-2398, VARIANTS LEU-2092 AND ALA-2365.
[16]	"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: 3841204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1937-2018 AND 3811-4334, VARIANTS PHE-3949; TYR-3964 AND GLU-4181.
[17]	"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: 3621347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2115-2179. Tissue: Small intestine.
[18]	"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: 2450346] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2127-2179.
[19]	"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: 3426612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2129-2235.
[20]	"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: 2445342] [Abstract] Cited for: PROTEIN SEQUENCE OF 2169-2179.
[21]	"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: 3903660] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3056-3159.
[22]	"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: 2994225] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3109-4563.
[23]	"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: 2932736] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3728-4563, VARIANTS ILE-3732; PHE-3949; TYR-3964 AND GLU-4181.
[24]	"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: 3841481] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 3846-4298. Tissue: Liver.
[25]	"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: 3024665] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 4217-4563, VARIANT SER-4338.
[26]	"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: 3659919] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION OF APO-B48.
[27]	"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: 3773997] [Abstract] Cited for: DOMAINS.
[28]	"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: 3095664] [Abstract] Cited for: DOMAINS.
[29]	"Apolipoprotein B is a calcium binding protein." Dashti N., Lee D.M., Mok T. Biochem. Biophys. Res. Commun. 137:493-499(1986) [PubMed: 3087360] [Abstract] Cited for: CALCIUM-BINDING DATA.
[30]	"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: 10679026] [Abstract] Cited for: PALMITOYLATION AT CYS-1112.
[31]	"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: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3358, MASS SPECTROMETRY. Tissue: Plasma.
[32]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1523; ASN-2982; ASN-3465 AND ASN-3895, MASS SPECTROMETRY. Tissue: Plasma.
[33]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4507, MASS SPECTROMETRY. Tissue: Epithelium.
[34]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-928, 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: 19159218] [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]	"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: 1979313] [Abstract] Cited for: VARIANT SER-4338.
[37]	"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: 2563166] [Abstract] Cited for: VARIANT FDB GLN-3527.
[38]	"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: 2216805] [Abstract] Cited for: VARIANT LEU-2739.
[39]	"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: 7883971] [Abstract] Cited for: VARIANT FDB CYS-3558.
[40]	"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: 8889592] [Abstract] Cited for: VARIANTS LEU-1437; SER-1914; LYS-2566; THR-3121; ALA-3945; MET-4128 AND THR-4481.
[41]	"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: 9259199] [Abstract] Cited for: VARIANTS FDB GLN-3527 AND CYS-3558.
[42]	"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: 9490296] [Abstract] Cited for: VARIANTS SER-1914; ARG-1923; LEU-2739; ASP-3319; THR-3427; GLN-3432 AND ILE-3921.
[43]	"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: 12551903] [Abstract] Cited for: VARIANT FHBL TRP-490, VARIANT ILE-98, CHARACTERIZATION OF VARIANT TRP-490, MUTAGENESIS OF ASP-483 AND ARG-490.
[44]	"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: 14732481] [Abstract] Cited for: VARIANT HIS-1128.
[45]	"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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-2564.
+	Additional computationally mapped references.

Web resources

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Apolipoprotein B entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. 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.
UniGene	Hs.120759
3D structure databases
ModBase	Search...
PTM databases
GlycoSuiteDB	P04114.
PhosphoSite	P04114.
2-D gel databases
Cornea-2DPAGE	P04114.
Proteomic databases
PeptideAtlas	P04114.
PRIDE	P04114.
Genome annotation databases
Ensembl	ENSG00000084674. Homo sapiens. [Contig view]
GeneID	338.
KEGG	hsa:338.
Organism-specific databases
GeneCards	GC02M021135.
H-InvDB	HIX0024005.
HGNC	HGNC:603. APOB.
HPA	CAB016070.
MIM	107730. gene+phenotype. 144010. phenotype.
Orphanet	89. Defective apolipoprotein B-100, familial. 406. Hypercholesterolemia, familial.
PharmGKB	PA50.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P04114.
Enzyme and pathway databases
Pathway_Interaction_DB	amb2_neutrophils_pathway. amb2 Integrin signaling. hnf3apathway. FOXA1 transcription factor network.
Reactome	REACT_602. Lipid and lipoprotein metabolism. REACT_604. Hemostasis. REACT_6900. Signaling in Immune system.
Gene expression databases
ArrayExpress	P04114.
Bgee	P04114.
GermOnline	ENSG00000084674. Homo sapiens.
Family and domain databases
InterPro	IPR001747. Lipid_transpt_N. IPR009454. Lipid_transpt_open_b-sht. IPR015255. Vitellinogen_open_b-sht. IPR011030. Vitellinogen_superhlx. [Graphical view]
Gene3D	G3DSA:1.25.10.20. Vitellinogen_superhlx. 1 hit.
Pfam	PF06448. DUF1081. 1 hit. PF09172. DUF1943. 1 hit. PF01347. Vitellogenin_N. 1 hit. [Graphical view]
SMART	SM00638. LPD_N. 1 hit. [Graphical view]
PROSITE	PS51211. VITELLOGENIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB01076. Atorvastatin.
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, Q7Z600, Q9UMN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	June 16, 2009
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)