UniProtKB - P04114 (APOB_HUMAN)
Protein
Apolipoprotein B-100
Gene
APOB
Organism
Homo sapiens (Human)
Status
Functioni
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.
GO - Molecular functioni
- cholesterol transfer activity Source: BHF-UCL
- heparin binding Source: BHF-UCL
- lipase binding Source: BHF-UCL
- low-density lipoprotein particle receptor binding Source: BHF-UCL
- phospholipid binding Source: BHF-UCL
GO - Biological processi
- artery morphogenesis Source: Ensembl
- cellular protein metabolic process Source: Reactome
- cellular response to prostaglandin stimulus Source: Ensembl
- cellular response to tumor necrosis factor Source: Ensembl
- cholesterol efflux Source: Ensembl
- cholesterol homeostasis Source: BHF-UCL
- cholesterol metabolic process Source: BHF-UCL
- cholesterol transport Source: BHF-UCL
- chylomicron assembly Source: Reactome
- chylomicron remnant clearance Source: Reactome
- chylomicron remodeling Source: Reactome
- fertilization Source: Ensembl
- flagellated sperm motility Source: Ensembl
- in utero embryonic development Source: Ensembl
- leukocyte migration Source: Reactome
- lipoprotein biosynthetic process Source: Ensembl
- lipoprotein catabolic process Source: Ensembl
- lipoprotein transport Source: GO_Central
- low-density lipoprotein particle clearance Source: BHF-UCL
- low-density lipoprotein particle remodeling Source: BHF-UCL
- membrane organization Source: Reactome
- nervous system development Source: Ensembl
- positive regulation of cholesterol storage Source: BHF-UCL
- positive regulation of gene expression Source: Ensembl
- positive regulation of lipid storage Source: BHF-UCL
- positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
- post-embryonic development Source: Ensembl
- post-translational protein modification Source: Reactome
- receptor-mediated endocytosis Source: Reactome
- regulation of cholesterol biosynthetic process Source: Ensembl
- response to carbohydrate Source: Ensembl
- response to estradiol Source: Ensembl
- response to lipopolysaccharide Source: Ensembl
- response to selenium ion Source: Ensembl
- response to virus Source: UniProtKB
- retinoid metabolic process Source: Reactome
- spermatogenesis Source: Ensembl
- toll-like receptor signaling pathway Source: Reactome
- triglyceride catabolic process Source: Ensembl
- triglyceride mobilization Source: GO_Central
- very-low-density lipoprotein particle assembly Source: Reactome
- very-low-density lipoprotein particle clearance Source: Reactome
Keywordsi
Molecular function | Heparin-binding |
Biological process | Cholesterol metabolism, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport |
Enzyme and pathway databases
PathwayCommonsi | P04114 |
Reactomei | R-HSA-202733, Cell surface interactions at the vascular wall R-HSA-3000471, Scavenging by Class B Receptors R-HSA-3000480, Scavenging by Class A Receptors R-HSA-3000484, Scavenging by Class F Receptors R-HSA-3000497, Scavenging by Class H Receptors R-HSA-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-HSA-432142, Platelet sensitization by LDL R-HSA-5686938, Regulation of TLR by endogenous ligand R-HSA-8856825, Cargo recognition for clathrin-mediated endocytosis R-HSA-8856828, Clathrin-mediated endocytosis R-HSA-8866423, VLDL assembly R-HSA-8957275, Post-translational protein phosphorylation R-HSA-8963888, Chylomicron assembly R-HSA-8963901, Chylomicron remodeling R-HSA-8964026, Chylomicron clearance R-HSA-8964038, LDL clearance R-HSA-8964041, LDL remodeling R-HSA-8964046, VLDL clearance R-HSA-975634, Retinoid metabolism and transport |
SIGNORi | P04114 |
Names & Taxonomyi
Protein namesi | Recommended name: Apolipoprotein B-100Short name: Apo B-100 Cleaved into the following chain: |
Gene namesi | Name:APOB |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:603, APOB |
MIMi | 107730, gene |
neXtProti | NX_P04114 |
VEuPathDBi | HostDB:ENSG00000084674.13 |
Subcellular locationi
Extracellular region or secreted
- Secreted 2 Publications
Other locations
- Cytoplasm 1 Publication
- Lipid droplet 1 Publication
Cytosol
- cytosol Source: HPA
Endoplasmic reticulum
- endoplasmic reticulum exit site Source: UniProtKB
- endoplasmic reticulum lumen Source: Reactome
- endoplasmic reticulum membrane Source: Reactome
- smooth endoplasmic reticulum Source: Reactome
Endosome
- early endosome Source: Reactome
- endosome lumen Source: Reactome
- endosome membrane Source: Reactome
Extracellular region or secreted
- chylomicron Source: BHF-UCL
- chylomicron remnant Source: BHF-UCL
- extracellular exosome Source: UniProtKB
- extracellular region Source: BHF-UCL
- extracellular space Source: BHF-UCL
- high-density lipoprotein particle Source: Ensembl
- intermediate-density lipoprotein particle Source: BHF-UCL
- low-density lipoprotein particle Source: BHF-UCL
- mature chylomicron Source: BHF-UCL
- very-low-density lipoprotein particle Source: BHF-UCL
Lysosome
- lysosomal lumen Source: Reactome
Plasma Membrane
- plasma membrane Source: Reactome
Other locations
- clathrin-coated endocytic vesicle membrane Source: Reactome
- cytoplasm Source: UniProtKB
- endocytic vesicle lumen Source: Reactome
- intracellular membrane-bounded organelle Source: HPA
- lipid droplet Source: UniProtKB-SubCell
- neuronal cell body Source: MGI
- vesicle lumen Source: Ensembl
Keywords - Cellular componenti
Chylomicron, Cytoplasm, LDL, Lipid droplet, Secreted, VLDLPathology & Biotechi
Involvement in diseasei
Hypobetalipoproteinemia, familial, 1 (FHBL1)3 Publications
The disease is caused by variants 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).1 Publication
Disease descriptionA 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.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_022610 | 490 | R → W in FHBL1; reduced protein secretion. 1 PublicationCorresponds to variant dbSNP:rs771541567Ensembl. | 1 | |
Natural variantiVAR_076539 | 952 | V → L in FHBL1; unknown pathological significance; does not affect interaction with MTTP. 1 Publication | 1 |
Hypercholesterolemia, familial, 2 (FHCL2)4 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA form of hypercholesterolemia, a disorder of lipoprotein metabolism characterized by elevated serum low-density lipoprotein (LDL) cholesterol levels, which result in excess deposition of cholesterol in tissues and leads to xanthelasma, xanthomas, accelerated atherosclerosis and increased risk of premature coronary heart disease. FHCL2 inheritance is autosomal dominant.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_005025 | 3527 | R → Q in FHCL2. 3 PublicationsCorresponds to variant dbSNP:rs5742904Ensembl. | 1 | |
Natural variantiVAR_005026 | 3558 | R → C in FHCL2. 2 PublicationsCorresponds to variant dbSNP:rs12713559Ensembl. | 1 |
Defects in APOB associated with defects in other genes (polygenic) can contribute to hypocholesterolemia.
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 483 | D → N: Impairs protein secretion. 1 Publication | 1 | |
Mutagenesisi | 483 | D → Q: Does not affect protein secretion. 1 Publication | 1 | |
Mutagenesisi | 490 | R → A: Impairs protein secretion. 1 Publication | 1 | |
Mutagenesisi | 490 | R → K: Does not affect protein secretion. 1 Publication | 1 |
Keywords - Diseasei
Atherosclerosis, Disease variantOrganism-specific databases
DisGeNETi | 338 |
GeneReviewsi | APOB |
MalaCardsi | APOB |
MIMi | 144010, phenotype 615558, phenotype |
Orphaneti | 391665, Homozygous familial hypercholesterolemia 426, NON RARE IN EUROPE: Familial hypobetalipoproteinemia 406, NON RARE IN EUROPE: Heterozygous familial hypercholesterolemia |
PharmGKBi | PA50 |
Miscellaneous databases
Pharosi | P04114, Tchem |
Chemistry databases
ChEMBLi | CHEMBL4549 |
DrugBanki | DB14533, Zinc chloride DB14548, Zinc sulfate, unspecified form |
Genetic variation databases
BioMutai | APOB |
DMDMi | 300669605 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 27 | Add BLAST | 27 | |
ChainiPRO_0000020750 | 28 – 4563 | Apolipoprotein B-100Add BLAST | 4536 | |
ChainiPRO_0000020751 | 28 – 2179 | Apolipoprotein B-48Add BLAST | 2152 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 34 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 39 ↔ 88 | PROSITE-ProRule annotation1 Publication | ||
Disulfide bondi | 78 ↔ 97 | PROSITE-ProRule annotation1 Publication | ||
Glycosylationi | 185 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 186 ↔ 212 | PROSITE-ProRule annotation1 Publication | ||
Disulfide bondi | 245 ↔ 261 | PROSITE-ProRule annotation1 Publication | ||
Disulfide bondi | 385 ↔ 390 | PROSITE-ProRule annotation1 Publication | ||
Disulfide bondi | 478 ↔ 513 | PROSITE-ProRule annotation1 Publication | ||
Disulfide bondi | 966 ↔ 976 | PROSITE-ProRule annotation1 Publication | ||
Glycosylationi | 983 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Lipidationi | 1112 | S-palmitoyl cysteine1 Publication | 1 | |
Glycosylationi | 1368 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1377 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1523 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Modified residuei | 2004 | N6-acetyllysineCombined sources | 1 | |
Glycosylationi | 2239 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 2560 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2779 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 2982 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Glycosylationi | 3101 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 3194 ↔ 3324 | PROSITE-ProRule annotation1 Publication | ||
Glycosylationi | 3224 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Modified residuei | 3279 | PhosphoserineCombined sources | 1 | |
Glycosylationi | 3336 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3358 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 3411 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 3465 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Glycosylationi | 3895 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Modified residuei | 4048 | Phosphoserine; by FAM20CCombined sources1 Publication | 1 | |
Modified residuei | 4052 | PhosphothreonineCombined sources | 1 | |
Glycosylationi | 4237 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 4431 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Post-translational modificationi
Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle.1 Publication
Keywords - PTMi
Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, PhosphoproteinProteomic databases
CPTACi | CPTAC-1299 CPTAC-1300 CPTAC-2205 CPTAC-652 CPTAC-653 non-CPTAC-1080 non-CPTAC-1081 non-CPTAC-1082 |
EPDi | P04114 |
jPOSTi | P04114 |
MassIVEi | P04114 |
MaxQBi | P04114 |
PaxDbi | P04114 |
PeptideAtlasi | P04114 |
PRIDEi | P04114 |
ProteomicsDBi | 51654 |
PTM databases
CarbonylDBi | P04114 |
GlyConnecti | 57, 57 N-Linked glycans (13 sites) |
GlyGeni | P04114, 28 sites, 20 N-linked glycans (8 sites), 1 O-linked glycan (7 sites) |
iPTMneti | P04114 |
PhosphoSitePlusi | P04114 |
SwissPalmi | P04114 |
Expressioni
Inductioni
Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication
Gene expression databases
Bgeei | ENSG00000084674, Expressed in jejunal mucosa and 102 other tissues |
ExpressionAtlasi | P04114, baseline and differential |
Genevisiblei | P04114, HS |
Organism-specific databases
HPAi | ENSG00000084674, Group enriched (intestine, liver) |
Interactioni
Subunit structurei
Binary interactionsi
Hide detailsP04114
GO - Molecular functioni
- lipase binding Source: BHF-UCL
- low-density lipoprotein particle receptor binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 106835, 85 interactors |
DIPi | DIP-44767N |
IntActi | P04114, 60 interactors |
MINTi | P04114 |
STRINGi | 9606.ENSP00000233242 |
Chemistry databases
BindingDBi | P04114 |
Miscellaneous databases
RNActi | P04114, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 46 – 672 | VitellogeninPROSITE-ProRule annotationAdd BLAST | 627 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 32 – 126 | Heparin-bindingAdd BLAST | 95 | |
Regioni | 232 – 306 | Heparin-bindingAdd BLAST | 75 | |
Regioni | 902 – 959 | Heparin-bindingAdd BLAST | 58 | |
Regioni | 2043 – 2178 | Heparin-bindingAdd BLAST | 136 | |
Regioni | 3161 – 3236 | Heparin-bindingAdd BLAST | 76 | |
Regioni | 3174 – 3184 | Basic (possible receptor binding region)Add BLAST | 11 | |
Regioni | 3373 – 3393 | LDL receptor bindingAdd BLAST | 21 | |
Regioni | 3383 – 3516 | Heparin-bindingAdd BLAST | 134 | |
Regioni | 3386 – 3394 | Basic (possible receptor binding region) | 9 |
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG4338, Eukaryota |
InParanoidi | P04114 |
OrthoDBi | 5350at2759 |
PhylomeDBi | P04114 |
TreeFami | TF331316 |
Family and domain databases
Gene3Di | 1.25.10.20, 1 hit 2.30.230.10, 1 hit |
InterProi | View protein in InterPro IPR022176, ApoB100_C IPR016024, ARM-type_fold IPR015819, Lipid_transp_b-sht_shell IPR001747, Lipid_transpt_N IPR009454, Lipid_transpt_open_b-sht IPR011030, Lipovitellin_superhlx_dom IPR015816, Vitellinogen_b-sht_N IPR015255, Vitellinogen_open_b-sht |
Pfami | View protein in Pfam PF12491, ApoB100_C, 1 hit PF06448, DUF1081, 1 hit PF09172, DUF1943, 1 hit PF01347, Vitellogenin_N, 1 hit |
SMARTi | View protein in SMART SM01169, DUF1943, 1 hit SM00638, LPD_N, 1 hit |
SUPFAMi | SSF48371, SSF48371, 1 hit SSF48431, SSF48431, 1 hit SSF56968, SSF56968, 2 hits |
PROSITEi | View protein in PROSITE PS51211, VITELLOGENIN, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
P04114-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDPPRPALLA LLALPALLLL LLAGARAEEE MLENVSLVCP KDATRFKHLR
60 70 80 90 100
KYTYNYEAES SSGVPGTADS RSATRINCKV ELEVPQLCSF ILKTSQCTLK
110 120 130 140 150
EVYGFNPEGK ALLKKTKNSE EFAAAMSRYE LKLAIPEGKQ VFLYPEKDEP
160 170 180 190 200
TYILNIKRGI ISALLVPPET EEAKQVLFLD TVYGNCSTHF TVKTRKGNVA
210 220 230 240 250
TEISTERDLG QCDRFKPIRT GISPLALIKG MTRPLSTLIS SSQSCQYTLD
260 270 280 290 300
AKRKHVAEAI CKEQHLFLPF SYKNKYGMVA QVTQTLKLED TPKINSRFFG
310 320 330 340 350
EGTKKMGLAF ESTKSTSPPK QAEAVLKTLQ ELKKLTISEQ NIQRANLFNK
360 370 380 390 400
LVTELRGLSD EAVTSLLPQL IEVSSPITLQ ALVQCGQPQC STHILQWLKR
410 420 430 440 450
VHANPLLIDV VTYLVALIPE PSAQQLREIF NMARDQRSRA TLYALSHAVN
460 470 480 490 500
NYHKTNPTGT QELLDIANYL MEQIQDDCTG DEDYTYLILR VIGNMGQTME
510 520 530 540 550
QLTPELKSSI LKCVQSTKPS LMIQKAAIQA LRKMEPKDKD QEVLLQTFLD
560 570 580 590 600
DASPGDKRLA AYLMLMRSPS QADINKIVQI LPWEQNEQVK NFVASHIANI
610 620 630 640 650
LNSEELDIQD LKKLVKEALK ESQLPTVMDF RKFSRNYQLY KSVSLPSLDP
660 670 680 690 700
ASAKIEGNLI FDPNNYLPKE SMLKTTLTAF GFASADLIEI GLEGKGFEPT
710 720 730 740 750
LEALFGKQGF FPDSVNKALY WVNGQVPDGV SKVLVDHFGY TKDDKHEQDM
760 770 780 790 800
VNGIMLSVEK LIKDLKSKEV PEARAYLRIL GEELGFASLH DLQLLGKLLL
810 820 830 840 850
MGARTLQGIP QMIGEVIRKG SKNDFFLHYI FMENAFELPT GAGLQLQISS
860 870 880 890 900
SGVIAPGAKA GVKLEVANMQ AELVAKPSVS VEFVTNMGII IPDFARSGVQ
910 920 930 940 950
MNTNFFHESG LEAHVALKAG KLKFIIPSPK RPVKLLSGGN TLHLVSTTKT
960 970 980 990 1000
EVIPPLIENR QSWSVCKQVF PGLNYCTSGA YSNASSTDSA SYYPLTGDTR
1010 1020 1030 1040 1050
LELELRPTGE IEQYSVSATY ELQREDRALV DTLKFVTQAE GAKQTEATMT
1060 1070 1080 1090 1100
FKYNRQSMTL SSEVQIPDFD VDLGTILRVN DESTEGKTSY RLTLDIQNKK
1110 1120 1130 1140 1150
ITEVALMGHL SCDTKEERKI KGVISIPRLQ AEARSEILAH WSPAKLLLQM
1160 1170 1180 1190 1200
DSSATAYGST VSKRVAWHYD EEKIEFEWNT GTNVDTKKMT SNFPVDLSDY
1210 1220 1230 1240 1250
PKSLHMYANR LLDHRVPQTD MTFRHVGSKL IVAMSSWLQK ASGSLPYTQT
1260 1270 1280 1290 1300
LQDHLNSLKE FNLQNMGLPD FHIPENLFLK SDGRVKYTLN KNSLKIEIPL
1310 1320 1330 1340 1350
PFGGKSSRDL KMLETVRTPA LHFKSVGFHL PSREFQVPTF TIPKLYQLQV
1360 1370 1380 1390 1400
PLLGVLDLST NVYSNLYNWS ASYSGGNTST DHFSLRARYH MKADSVVDLL
1410 1420 1430 1440 1450
SYNVQGSGET TYDHKNTFTL SYDGSLRHKF LDSNIKFSHV EKLGNNPVSK
1460 1470 1480 1490 1500
GLLIFDASSS WGPQMSASVH LDSKKKQHLF VKEVKIDGQF RVSSFYAKGT
1510 1520 1530 1540 1550
YGLSCQRDPN TGRLNGESNL RFNSSYLQGT NQITGRYEDG TLSLTSTSDL
1560 1570 1580 1590 1600
QSGIIKNTAS LKYENYELTL KSDTNGKYKN FATSNKMDMT FSKQNALLRS
1610 1620 1630 1640 1650
EYQADYESLR FFSLLSGSLN SHGLELNADI LGTDKINSGA HKATLRIGQD
1660 1670 1680 1690 1700
GISTSATTNL KCSLLVLENE LNAELGLSGA SMKLTTNGRF REHNAKFSLD
1710 1720 1730 1740 1750
GKAALTELSL GSAYQAMILG VDSKNIFNFK VSQEGLKLSN DMMGSYAEMK
1760 1770 1780 1790 1800
FDHTNSLNIA GLSLDFSSKL DNIYSSDKFY KQTVNLQLQP YSLVTTLNSD
1810 1820 1830 1840 1850
LKYNALDLTN NGKLRLEPLK LHVAGNLKGA YQNNEIKHIY AISSAALSAS
1860 1870 1880 1890 1900
YKADTVAKVQ GVEFSHRLNT DIAGLASAID MSTNYNSDSL HFSNVFRSVM
1910 1920 1930 1940 1950
APFTMTIDAH TNGNGKLALW GEHTGQLYSK FLLKAEPLAF TFSHDYKGST
1960 1970 1980 1990 2000
SHHLVSRKSI SAALEHKVSA LLTPAEQTGT WKLKTQFNNN EYSQDLDAYN
2010 2020 2030 2040 2050
TKDKIGVELT GRTLADLTLL DSPIKVPLLL SEPINIIDAL EMRDAVEKPQ
2060 2070 2080 2090 2100
EFTIVAFVKY DKNQDVHSIN LPFFETLQEY FERNRQTIIV VLENVQRNLK
2110 2120 2130 2140 2150
HINIDQFVRK YRAALGKLPQ QANDYLNSFN WERQVSHAKE KLTALTKKYR
2160 2170 2180 2190 2200
ITENDIQIAL DDAKINFNEK LSQLQTYMIQ FDQYIKDSYD LHDLKIAIAN
2210 2220 2230 2240 2250
IIDEIIEKLK SLDEHYHIRV NLVKTIHDLH LFIENIDFNK SGSSTASWIQ
2260 2270 2280 2290 2300
NVDTKYQIRI QIQEKLQQLK RHIQNIDIQH LAGKLKQHIE AIDVRVLLDQ
2310 2320 2330 2340 2350
LGTTISFERI NDILEHVKHF VINLIGDFEV AEKINAFRAK VHELIERYEV
2360 2370 2380 2390 2400
DQQIQVLMDK LVELAHQYKL KETIQKLSNV LQQVKIKDYF EKLVGFIDDA
2410 2420 2430 2440 2450
VKKLNELSFK TFIEDVNKFL DMLIKKLKSF DYHQFVDETN DKIREVTQRL
2460 2470 2480 2490 2500
NGEIQALELP QKAEALKLFL EETKATVAVY LESLQDTKIT LIINWLQEAL
2510 2520 2530 2540 2550
SSASLAHMKA KFRETLEDTR DRMYQMDIQQ ELQRYLSLVG QVYSTLVTYI
2560 2570 2580 2590 2600
SDWWTLAAKN LTDFAEQYSI QDWAKRMKAL VEQGFTVPEI KTILGTMPAF
2610 2620 2630 2640 2650
EVSLQALQKA TFQTPDFIVP LTDLRIPSVQ INFKDLKNIK IPSRFSTPEF
2660 2670 2680 2690 2700
TILNTFHIPS FTIDFVEMKV KIIRTIDQML NSELQWPVPD IYLRDLKVED
2710 2720 2730 2740 2750
IPLARITLPD FRLPEIAIPE FIIPTLNLND FQVPDLHIPE FQLPHISHTI
2760 2770 2780 2790 2800
EVPTFGKLYS ILKIQSPLFT LDANADIGNG TTSANEAGIA ASITAKGESK
2810 2820 2830 2840 2850
LEVLNFDFQA NAQLSNPKIN PLALKESVKF SSKYLRTEHG SEMLFFGNAI
2860 2870 2880 2890 2900
EGKSNTVASL HTEKNTLELS NGVIVKINNQ LTLDSNTKYF HKLNIPKLDF
2910 2920 2930 2940 2950
SSQADLRNEI KTLLKAGHIA WTSSGKGSWK WACPRFSDEG THESQISFTI
2960 2970 2980 2990 3000
EGPLTSFGLS NKINSKHLRV NQNLVYESGS LNFSKLEIQS QVDSQHVGHS
3010 3020 3030 3040 3050
VLTAKGMALF GEGKAEFTGR HDAHLNGKVI GTLKNSLFFS AQPFEITAST
3060 3070 3080 3090 3100
NNEGNLKVRF PLRLTGKIDF LNNYALFLSP SAQQASWQVS ARFNQYKYNQ
3110 3120 3130 3140 3150
NFSAGNNENI MEAHVGINGE ANLDFLNIPL TIPEMRLPYT IITTPPLKDF
3160 3170 3180 3190 3200
SLWEKTGLKE FLKTTKQSFD LSVKAQYKKN KHRHSITNPL AVLCEFISQS
3210 3220 3230 3240 3250
IKSFDRHFEK NRNNALDFVT KSYNETKIKF DKYKAEKSHD ELPRTFQIPG
3260 3270 3280 3290 3300
YTVPVVNVEV SPFTIEMSAF GYVFPKAVSM PSFSILGSDV RVPSYTLILP
3310 3320 3330 3340 3350
SLELPVLHVP RNLKLSLPDF KELCTISHIF IPAMGNITYD FSFKSSVITL
3360 3370 3380 3390 3400
NTNAELFNQS DIVAHLLSSS SSVIDALQYK LEGTTRLTRK RGLKLATALS
3410 3420 3430 3440 3450
LSNKFVEGSH NSTVSLTTKN MEVSVATTTK AQIPILRMNF KQELNGNTKS
3460 3470 3480 3490 3500
KPTVSSSMEF KYDFNSSMLY STAKGAVDHK LSLESLTSYF SIESSTKGDV
3510 3520 3530 3540 3550
KGSVLSREYS GTIASEANTY LNSKSTRSSV KLQGTSKIDD IWNLEVKENF
3560 3570 3580 3590 3600
AGEATLQRIY SLWEHSTKNH LQLEGLFFTN GEHTSKATLE LSPWQMSALV
3610 3620 3630 3640 3650
QVHASQPSSF HDFPDLGQEV ALNANTKNQK IRWKNEVRIH SGSFQSQVEL
3660 3670 3680 3690 3700
SNDQEKAHLD IAGSLEGHLR FLKNIILPVY DKSLWDFLKL DVTTSIGRRQ
3710 3720 3730 3740 3750
HLRVSTAFVY TKNPNGYSFS IPVKVLADKF IIPGLKLNDL NSVLVMPTFH
3760 3770 3780 3790 3800
VPFTDLQVPS CKLDFREIQI YKKLRTSSFA LNLPTLPEVK FPEVDVLTKY
3810 3820 3830 3840 3850
SQPEDSLIPF FEITVPESQL TVSQFTLPKS VSDGIAALDL NAVANKIADF
3860 3870 3880 3890 3900
ELPTIIVPEQ TIEIPSIKFS VPAGIVIPSF QALTARFEVD SPVYNATWSA
3910 3920 3930 3940 3950
SLKNKADYVE TVLDSTCSST VQFLEYELNV LGTHKIEDGT LASKTKGTFA
3960 3970 3980 3990 4000
HRDFSAEYEE DGKYEGLQEW EGKAHLNIKS PAFTDLHLRY QKDKKGISTS
4010 4020 4030 4040 4050
AASPAVGTVG MDMDEDDDFS KWNFYYSPQS SPDKKLTIFK TELRVRESDE
4060 4070 4080 4090 4100
ETQIKVNWEE EAASGLLTSL KDNVPKATGV LYDYVNKYHW EHTGLTLREV
4110 4120 4130 4140 4150
SSKLRRNLQN NAEWVYQGAI RQIDDIDVRF QKAASGTTGT YQEWKDKAQN
4160 4170 4180 4190 4200
LYQELLTQEG QASFQGLKDN VFDGLVRVTQ EFHMKVKHLI DSLIDFLNFP
4210 4220 4230 4240 4250
RFQFPGKPGI YTREELCTMF IREVGTVLSQ VYSKVHNGSE ILFSYFQDLV
4260 4270 4280 4290 4300
ITLPFELRKH KLIDVISMYR ELLKDLSKEA QEVFKAIQSL KTTEVLRNLQ
4310 4320 4330 4340 4350
DLLQFIFQLI EDNIKQLKEM KFTYLINYIQ DEINTIFSDY IPYVFKLLKE
4360 4370 4380 4390 4400
NLCLNLHKFN EFIQNELQEA SQELQQIHQY IMALREEYFD PSIVGWTVKY
4410 4420 4430 4440 4450
YELEEKIVSL IKNLLVALKD FHSEYIVSAS NFTSQLSSQV EQFLHRNIQE
4460 4470 4480 4490 4500
YLSILTDPDG KGKEKIAELS ATAQEIIKSQ AIATKKIISD YHQQFRYKLQ
4510 4520 4530 4540 4550
DFSDQLSDYY EKFIAESKRL IDLSIQNYHT FLIYITELLK KLQSTTVMNP
4560
YMKLAPGELT IIL
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA8MUN2 | A8MUN2_HUMAN | Apolipoprotein B-100 | APOB | 828 | Annotation score: | ||
A0A669KB70 | A0A669KB70_HUMAN | Apolipoprotein B-100 | APOB | 135 | Annotation score: |
Sequence cautioni
The sequence AAA51752 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 11 – 13 | Missing in AAB60718 (PubMed:3030729).Curated | 3 | |
Sequence conflicti | 11 – 13 | Missing in CAA28420 (PubMed:3030729).Curated | 3 | |
Sequence conflicti | 329 | L → V in AAA35549 (PubMed:3759943).Curated | 1 | |
Sequence conflicti | 645 | L → I in AAA35549 (PubMed:3759943).Curated | 1 | |
Sequence conflicti | 704 | L → P in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 792 – 809 | LQLLG…TLQGI → SSSWKAASHGCPHSAGD in AAA51759 (PubMed:3860836).CuratedAdd BLAST | 18 | |
Sequence conflicti | 793 | Q → R in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 893 | D → K AA sequence (PubMed:6373369).Curated | 1 | |
Sequence conflicti | 919 | A → P in AAA35549 (PubMed:3759943).Curated | 1 | |
Sequence conflicti | 1109 | H → D in CAA28420 (PubMed:3030729).Curated | 1 | |
Sequence conflicti | 1180 | T → R in AAA51752 (PubMed:3461454).Curated | 1 | |
Sequence conflicti | 1271 | F → S in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 1418 | F → S in CAA28420 (PubMed:3030729).Curated | 1 | |
Sequence conflicti | 1445 | N → I in AAA51752 (PubMed:3461454).Curated | 1 | |
Sequence conflicti | 1535 | G → E in AAA51752 (PubMed:3461454).Curated | 1 | |
Sequence conflicti | 1867 | R → G in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 2098 | N → K in CAA28420 (PubMed:3030729).Curated | 1 | |
Sequence conflicti | 2218 | I → T in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 2221 | N → I in CAA28420 (PubMed:3030729).Curated | 1 | |
Sequence conflicti | 2324 – 2326 | LIG → PYW in AAA51741 (PubMed:3676265).Curated | 3 | |
Sequence conflicti | 2353 | Q → H in AAA51741 (PubMed:3676265).Curated | 1 | |
Sequence conflicti | 2540 | G → S in CAA28420 (PubMed:3030729).Curated | 1 | |
Sequence conflicti | 2718 – 2737 | Missing in AAA51758 (PubMed:2883086).CuratedAdd BLAST | 20 | |
Sequence conflicti | 2933 | C → S in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 3114 | H → L AA sequence (PubMed:6373369).Curated | 1 | |
Sequence conflicti | 3131 | T → R AA sequence (PubMed:6373369).Curated | 1 | |
Sequence conflicti | 3134 | E → P AA sequence (PubMed:6373369).Curated | 1 | |
Sequence conflicti | 3137 | L → R AA sequence (PubMed:6373369).Curated | 1 | |
Sequence conflicti | 3239 | H → Q in CAA28420 (PubMed:3030729).Curated | 1 | |
Sequence conflicti | 3286 | L → I in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 3291 | R → L in AAA51758 (PubMed:2883086).Curated | 1 | |
Sequence conflicti | 3337 | I → N in AAA51758 (PubMed:2883086).Curated | 1 | |
Sequence conflicti | 3431 | A → P in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 3728 | D → N in AAA51742 (PubMed:2932736).Curated | 1 | |
Sequence conflicti | 3782 | N → T in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 3824 | Q → R in CAA28420 (PubMed:3030729).Curated | 1 | |
Sequence conflicti | 3824 | Q → R in AAA51750 (PubMed:2994225).Curated | 1 | |
Sequence conflicti | 3876 | V → A in AAA35549 (PubMed:3759943).Curated | 1 | |
Sequence conflicti | 3876 | V → A in AAA51742 (PubMed:2932736).Curated | 1 | |
Sequence conflicti | 3911 | T → Y AA sequence (PubMed:2115173).Curated | 1 | |
Sequence conflicti | 3983 | F → S in AAA51742 (PubMed:2932736).Curated | 1 | |
Sequence conflicti | 4002 | A → P in AAA51742 (PubMed:2932736).Curated | 1 | |
Sequence conflicti | 4110 – 4111 | NN → DH in AAA35549 (PubMed:3759943).Curated | 2 | |
Sequence conflicti | 4110 – 4111 | NN → DH in AAA51742 (PubMed:2932736).Curated | 2 | |
Sequence conflicti | 4122 | Q → E in AAA35549 (PubMed:3759943).Curated | 1 | |
Sequence conflicti | 4122 | Q → E in AAA51742 (PubMed:2932736).Curated | 1 | |
Sequence conflicti | 4128 | V → E in AAA35549 (PubMed:3759943).Curated | 1 | |
Sequence conflicti | 4128 | V → E in AAA51742 (PubMed:2932736).Curated | 1 | |
Sequence conflicti | 4133 | A → G in AAA35549 (PubMed:3759943).Curated | 1 | |
Sequence conflicti | 4133 | A → G in AAA51742 (PubMed:2932736).Curated | 1 | |
Sequence conflicti | 4188 | H → K in AAB04636 (PubMed:3464946).Curated | 1 | |
Sequence conflicti | 4217 – 4218 | CT → FP in AAA35548 (PubMed:3024665).Curated | 2 | |
Sequence conflicti | 4221 | I → M in AAB04636 (PubMed:3464946).Curated | 1 |
RNA editingi
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.
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.
Polymorphismi
Genetic variations in APOB define the low density lipoprotein cholesterol level quantitative trait locus 4 (LDLCQ4) [MIMi:615558].
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_067277 | 12 – 14 | Missing 1 Publication | 3 | |
Natural variantiVAR_016184 | 98 | T → I Influences plasma concentrations of low density lipoprotein cholesterol. 6 PublicationsCorresponds to variant dbSNP:rs1367117Ensembl. | 1 | |
Natural variantiVAR_022036 | 103 | Y → H. Corresponds to variant dbSNP:rs9282603Ensembl. | 1 | |
Natural variantiVAR_022037 | 145 | P → S. Corresponds to variant dbSNP:rs6752026Ensembl. | 1 | |
Natural variantiVAR_056737 | 194 | T → M. Corresponds to variant dbSNP:rs13306198EnsemblClinVar. | 1 | |
Natural variantiVAR_076538 | 251 | A → T Does not affect plasma lipid levels. 1 PublicationCorresponds to variant dbSNP:rs61741625EnsemblClinVar. | 1 | |
Natural variantiVAR_019827 | 273 | K → N1 Publication | 1 | |
Natural variantiVAR_029341 | 408 | I → T. Corresponds to variant dbSNP:rs12714225Ensembl. | 1 | |
Natural variantiVAR_022610 | 490 | R → W in FHBL1; reduced protein secretion. 1 PublicationCorresponds to variant dbSNP:rs771541567Ensembl. | 1 | |
Natural variantiVAR_020135 | 554 | P → L. Corresponds to variant dbSNP:rs12714214Ensembl. | 1 | |
Natural variantiVAR_019828 | 618 | A → V3 PublicationsCorresponds to variant dbSNP:rs679899Ensembl. | 1 | |
Natural variantiVAR_020136 | 730 | V → I1 PublicationCorresponds to variant dbSNP:rs12691202Ensembl. | 1 | |
Natural variantiVAR_016185 | 733 | V → I. Corresponds to variant dbSNP:rs1800476Ensembl. | 1 | |
Natural variantiVAR_020137 | 741 | T → N. Corresponds to variant dbSNP:rs12714192Ensembl. | 1 | |
Natural variantiVAR_029342 | 877 | P → L. Corresponds to variant dbSNP:rs12714097EnsemblClinVar. | 1 | |
Natural variantiVAR_076539 | 952 | V → L in FHBL1; unknown pathological significance; does not affect interaction with MTTP. 1 Publication | 1 | |
Natural variantiVAR_056738 | 955 | P → S. Corresponds to variant dbSNP:rs13306206Ensembl. | 1 | |
Natural variantiVAR_029343 | 1086 | G → S. Corresponds to variant dbSNP:rs12720801EnsemblClinVar. | 1 | |
Natural variantiVAR_029344 | 1113 | D → H. Corresponds to variant dbSNP:rs12713844Ensembl. | 1 | |
Natural variantiVAR_022611 | 1128 | R → H1 PublicationCorresponds to variant dbSNP:rs12713843EnsemblClinVar. | 1 | |
Natural variantiVAR_019829 | 1218 | Q → E2 PublicationsCorresponds to variant dbSNP:rs1041956Ensembl. | 1 | |
Natural variantiVAR_029345 | 1388 | R → H. Corresponds to variant dbSNP:rs13306187EnsemblClinVar. | 1 | |
Natural variantiVAR_061558 | 1422 | Y → C8 PublicationsCorresponds to variant dbSNP:rs568413Ensembl. | 1 | |
Natural variantiVAR_005016 | 1437 | F → L1 PublicationCorresponds to variant dbSNP:rs1801697EnsemblClinVar. | 1 | |
Natural variantiVAR_067278 | 1613 | S → T1 PublicationCorresponds to variant dbSNP:rs61742247EnsemblClinVar. | 1 | |
Natural variantiVAR_068911 | 1670 | E → D2 PublicationsCorresponds to variant dbSNP:rs773681906Ensembl. | 1 | |
Natural variantiVAR_005017 | 1914 | N → S2 PublicationsCorresponds to variant dbSNP:rs1801699Ensembl. | 1 | |
Natural variantiVAR_005018 | 1923 | H → R2 PublicationsCorresponds to variant dbSNP:rs533617Ensembl. | 1 | |
Natural variantiVAR_068912 | 2037 | I → N2 Publications | 1 | |
Natural variantiVAR_019830 | 2092 | L → V1 PublicationCorresponds to variant dbSNP:rs1041960Ensembl. | 1 | |
Natural variantiVAR_029346 | 2299 | D → H. Corresponds to variant dbSNP:rs12713681Ensembl. | 1 | |
Natural variantiVAR_059582 | 2313 | I → V8 PublicationsCorresponds to variant dbSNP:rs584542Ensembl. | 1 | |
Natural variantiVAR_019831 | 2365 | A → T1 PublicationCorresponds to variant dbSNP:rs1041971Ensembl. | 1 | |
Natural variantiVAR_020138 | 2456 | A → D. Corresponds to variant dbSNP:rs12713675Ensembl. | 1 | |
Natural variantiVAR_035795 | 2564 | F → C in a colorectal cancer sample; somatic mutation; confirmed at protein level. 2 Publications | 1 | |
Natural variantiVAR_005019 | 2566 | E → K3 PublicationsCorresponds to variant dbSNP:rs1801696EnsemblClinVar. | 1 | |
Natural variantiVAR_019832 | 2680 | L → Q1 PublicationCorresponds to variant dbSNP:rs1042013Ensembl. | 1 | |
Natural variantiVAR_005020 | 2739 | P → L3 PublicationsCorresponds to variant dbSNP:rs676210Ensembl. | 1 | |
Natural variantiVAR_022038 | 2785 | N → H. Corresponds to variant dbSNP:rs2163204EnsemblClinVar. | 1 | |
Natural variantiVAR_005021 | 3121 | A → T1 PublicationCorresponds to variant dbSNP:rs1801694Ensembl. | 1 | |
Natural variantiVAR_029347 | 3182 | H → N. Corresponds to variant dbSNP:rs12720848EnsemblClinVar. | 1 | |
Natural variantiVAR_029348 | 3279 | S → G. Corresponds to variant dbSNP:rs12720854Ensembl. | 1 | |
Natural variantiVAR_020139 | 3294 | S → P. Corresponds to variant dbSNP:rs12720855Ensembl. | 1 | |
Natural variantiVAR_005022 | 3319 | D → H8 PublicationsCorresponds to variant dbSNP:rs1042021Ensembl. | 1 | |
Natural variantiVAR_005023 | 3427 | T → K8 PublicationsCorresponds to variant dbSNP:rs1042022Ensembl. | 1 | |
Natural variantiVAR_005024 | 3432 | Q → E8 PublicationsCorresponds to variant dbSNP:rs1042023Ensembl. | 1 | |
Natural variantiVAR_005025 | 3527 | R → Q in FHCL2. 3 PublicationsCorresponds to variant dbSNP:rs5742904Ensembl. | 1 | |
Natural variantiVAR_005026 | 3558 | R → C in FHCL2. 2 PublicationsCorresponds to variant dbSNP:rs12713559Ensembl. | 1 | |
Natural variantiVAR_016186 | 3638 | R → Q1 PublicationCorresponds to variant dbSNP:rs1801701Ensembl. | 1 | |
Natural variantiVAR_019833 | 3732 | I → T4 PublicationsCorresponds to variant dbSNP:rs1042025Ensembl. | 1 | |
Natural variantiVAR_029349 | 3801 | S → T. Corresponds to variant dbSNP:rs12713540Ensembl. | 1 | |
Natural variantiVAR_067279 | 3835 | I → L1 PublicationCorresponds to variant dbSNP:rs776119459Ensembl. | 1 | |
Natural variantiVAR_005027 | 3921 | V → I1 PublicationCorresponds to variant dbSNP:rs72654409Ensembl. | 1 | |
Natural variantiVAR_005028 | 3945 | T → A1 PublicationCorresponds to variant dbSNP:rs1801698EnsemblClinVar. | 1 | |
Natural variantiVAR_019834 | 3949 | F → L5 PublicationsCorresponds to variant dbSNP:rs1042027Ensembl. | 1 | |
Natural variantiVAR_019835 | 3964 | Y → F4 PublicationsCorresponds to variant dbSNP:rs1126468Ensembl. | 1 | |
Natural variantiVAR_005029 | 4128 | V → M1 PublicationCorresponds to variant dbSNP:rs1801703Ensembl. | 1 | |
Natural variantiVAR_016187 | 4181 | E → K6 PublicationsCorresponds to variant dbSNP:rs1042031Ensembl. | 1 | |
Natural variantiVAR_016188 | 4270 | R → T1 PublicationCorresponds to variant dbSNP:rs1801702Ensembl. | 1 | |
Natural variantiVAR_067280 | 4314 | I → V1 PublicationCorresponds to variant dbSNP:rs72654423Ensembl. | 1 | |
Natural variantiVAR_005030 | 4338 | S → N11 PublicationsCorresponds to variant dbSNP:rs1042034Ensembl. | 1 | |
Natural variantiVAR_029350 | 4394 | V → A. Corresponds to variant dbSNP:rs12720843EnsemblClinVar. | 1 | |
Natural variantiVAR_005031 | 4481 | A → T2 PublicationsCorresponds to variant dbSNP:rs1801695Ensembl. | 1 | |
Natural variantiVAR_067281 | 4482 | I → V1 PublicationCorresponds to variant dbSNP:rs142702699EnsemblClinVar. | 1 | |
Natural variantiVAR_020140 | 4484 | T → M. Corresponds to variant dbSNP:rs12713450Ensembl. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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 |
CCDSi | CCDS1703.1 |
PIRi | A27850, LPHUB |
RefSeqi | NP_000375.2, NM_000384.2 |
Genome annotation databases
Ensembli | ENST00000233242; ENSP00000233242; ENSG00000084674 |
GeneIDi | 338 |
KEGGi | hsa:338 |
UCSCi | uc002red.3, human |
Keywords - Coding sequence diversityi
RNA editingSimilar proteinsi
Cross-referencesi
Web resourcesi
SHMPD The Singapore human mutation and polymorphism database |
Wikipedia Apolipoprotein B entry |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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 |
CCDSi | CCDS1703.1 |
PIRi | A27850, LPHUB |
RefSeqi | NP_000375.2, NM_000384.2 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
BioGRIDi | 106835, 85 interactors |
DIPi | DIP-44767N |
IntActi | P04114, 60 interactors |
MINTi | P04114 |
STRINGi | 9606.ENSP00000233242 |
Chemistry databases
BindingDBi | P04114 |
ChEMBLi | CHEMBL4549 |
DrugBanki | DB14533, Zinc chloride DB14548, Zinc sulfate, unspecified form |
PTM databases
CarbonylDBi | P04114 |
GlyConnecti | 57, 57 N-Linked glycans (13 sites) |
GlyGeni | P04114, 28 sites, 20 N-linked glycans (8 sites), 1 O-linked glycan (7 sites) |
iPTMneti | P04114 |
PhosphoSitePlusi | P04114 |
SwissPalmi | P04114 |
Genetic variation databases
BioMutai | APOB |
DMDMi | 300669605 |
Proteomic databases
CPTACi | CPTAC-1299 CPTAC-1300 CPTAC-2205 CPTAC-652 CPTAC-653 non-CPTAC-1080 non-CPTAC-1081 non-CPTAC-1082 |
EPDi | P04114 |
jPOSTi | P04114 |
MassIVEi | P04114 |
MaxQBi | P04114 |
PaxDbi | P04114 |
PeptideAtlasi | P04114 |
PRIDEi | P04114 |
ProteomicsDBi | 51654 |
Protocols and materials databases
ABCDi | P04114, 1 sequenced antibody |
Antibodypediai | 4232, 1067 antibodies |
Genome annotation databases
Ensembli | ENST00000233242; ENSP00000233242; ENSG00000084674 |
GeneIDi | 338 |
KEGGi | hsa:338 |
UCSCi | uc002red.3, human |
Organism-specific databases
CTDi | 338 |
DisGeNETi | 338 |
GeneCardsi | APOB |
GeneReviewsi | APOB |
HGNCi | HGNC:603, APOB |
HPAi | ENSG00000084674, Group enriched (intestine, liver) |
MalaCardsi | APOB |
MIMi | 107730, gene 144010, phenotype 615558, phenotype |
neXtProti | NX_P04114 |
Orphaneti | 391665, Homozygous familial hypercholesterolemia 426, NON RARE IN EUROPE: Familial hypobetalipoproteinemia 406, NON RARE IN EUROPE: Heterozygous familial hypercholesterolemia |
PharmGKBi | PA50 |
VEuPathDBi | HostDB:ENSG00000084674.13 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG4338, Eukaryota |
InParanoidi | P04114 |
OrthoDBi | 5350at2759 |
PhylomeDBi | P04114 |
TreeFami | TF331316 |
Enzyme and pathway databases
PathwayCommonsi | P04114 |
Reactomei | R-HSA-202733, Cell surface interactions at the vascular wall R-HSA-3000471, Scavenging by Class B Receptors R-HSA-3000480, Scavenging by Class A Receptors R-HSA-3000484, Scavenging by Class F Receptors R-HSA-3000497, Scavenging by Class H Receptors R-HSA-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-HSA-432142, Platelet sensitization by LDL R-HSA-5686938, Regulation of TLR by endogenous ligand R-HSA-8856825, Cargo recognition for clathrin-mediated endocytosis R-HSA-8856828, Clathrin-mediated endocytosis R-HSA-8866423, VLDL assembly R-HSA-8957275, Post-translational protein phosphorylation R-HSA-8963888, Chylomicron assembly R-HSA-8963901, Chylomicron remodeling R-HSA-8964026, Chylomicron clearance R-HSA-8964038, LDL clearance R-HSA-8964041, LDL remodeling R-HSA-8964046, VLDL clearance R-HSA-975634, Retinoid metabolism and transport |
SIGNORi | P04114 |
Miscellaneous databases
BioGRID-ORCSi | 338, 5 hits in 873 CRISPR screens |
ChiTaRSi | APOB, human |
GeneWikii | Apolipoprotein_B |
GenomeRNAii | 338 |
Pharosi | P04114, Tchem |
PROi | PR:P04114 |
RNActi | P04114, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000084674, Expressed in jejunal mucosa and 102 other tissues |
ExpressionAtlasi | P04114, baseline and differential |
Genevisiblei | P04114, HS |
Family and domain databases
Gene3Di | 1.25.10.20, 1 hit 2.30.230.10, 1 hit |
InterProi | View protein in InterPro IPR022176, ApoB100_C IPR016024, ARM-type_fold IPR015819, Lipid_transp_b-sht_shell IPR001747, Lipid_transpt_N IPR009454, Lipid_transpt_open_b-sht IPR011030, Lipovitellin_superhlx_dom IPR015816, Vitellinogen_b-sht_N IPR015255, Vitellinogen_open_b-sht |
Pfami | View protein in Pfam PF12491, ApoB100_C, 1 hit PF06448, DUF1081, 1 hit PF09172, DUF1943, 1 hit PF01347, Vitellogenin_N, 1 hit |
SMARTi | View protein in SMART SM01169, DUF1943, 1 hit SM00638, LPD_N, 1 hit |
SUPFAMi | SSF48371, SSF48371, 1 hit SSF48431, SSF48431, 1 hit SSF56968, SSF56968, 2 hits |
PROSITEi | View protein in PROSITE PS51211, VITELLOGENIN, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | APOB_HUMAN | |
Accessioni | P04114Primary (citable) accession number: P04114 Secondary accession number(s): O00502 Q9UMN0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1986 |
Last sequence update: | July 13, 2010 | |
Last modified: | February 10, 2021 | |
This is version 239 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | 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. |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot