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P04114

- APOB_HUMAN

UniProt

P04114 - APOB_HUMAN

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Protein

Apolipoprotein B-100

Gene

APOB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

  1. cholesterol transporter activity Source: BHF-UCL
  2. heparin binding Source: BHF-UCL
  3. lipase binding Source: BHF-UCL
  4. low-density lipoprotein particle receptor binding Source: BHF-UCL
  5. phospholipid binding Source: BHF-UCL

GO - Biological processi

  1. artery morphogenesis Source: Ensembl
  2. blood coagulation Source: Reactome
  3. cellular response to prostaglandin stimulus Source: Ensembl
  4. cellular response to tumor necrosis factor Source: Ensembl
  5. cholesterol efflux Source: Ensembl
  6. cholesterol homeostasis Source: BHF-UCL
  7. cholesterol metabolic process Source: BHF-UCL
  8. cholesterol transport Source: BHF-UCL
  9. fertilization Source: Ensembl
  10. in utero embryonic development Source: Ensembl
  11. leukocyte migration Source: Reactome
  12. lipoprotein biosynthetic process Source: Ensembl
  13. lipoprotein catabolic process Source: Ensembl
  14. lipoprotein metabolic process Source: Reactome
  15. lipoprotein transport Source: Ensembl
  16. low-density lipoprotein particle clearance Source: BHF-UCL
  17. low-density lipoprotein particle remodeling Source: BHF-UCL
  18. nervous system development Source: Ensembl
  19. phototransduction, visible light Source: Reactome
  20. positive regulation of cholesterol storage Source: BHF-UCL
  21. positive regulation of lipid storage Source: BHF-UCL
  22. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  23. post-embryonic development Source: Ensembl
  24. receptor-mediated endocytosis Source: Reactome
  25. regulation of cholesterol biosynthetic process Source: Ensembl
  26. response to carbohydrate Source: Ensembl
  27. response to lipopolysaccharide Source: Ensembl
  28. response to selenium ion Source: Ensembl
  29. response to virus Source: UniProtKB
  30. retinoid metabolic process Source: Reactome
  31. small molecule metabolic process Source: Reactome
  32. spermatogenesis Source: Ensembl
  33. sperm motility Source: Ensembl
  34. triglyceride catabolic process Source: Ensembl
  35. triglyceride mobilization Source: Ensembl
  36. very-low-density lipoprotein particle assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
REACT_163679. Scavenging by Class B Receptors.
REACT_163699. Scavenging by Class A Receptors.
REACT_163813. Scavenging by Class F Receptors.
REACT_164002. Scavenging by Class H Receptors.
REACT_23879. Platelet sensitization by LDL.
REACT_24968. Retinoid metabolism and transport.
REACT_6841. Chylomicron-mediated lipid transport.
REACT_6934. LDL-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein B-100
Short name:
Apo B-100
Cleaved into the following chain:
Apolipoprotein B-48
Short name:
Apo B-48
Gene namesi
Name:APOB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:603. APOB.

Subcellular locationi

Cytoplasm 1 Publication. Secreted 1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. chylomicron Source: BHF-UCL
  3. chylomicron remnant Source: BHF-UCL
  4. clathrin-coated endocytic vesicle membrane Source: Reactome
  5. cytoplasm Source: UniProtKB
  6. cytosol Source: Reactome
  7. early endosome Source: Reactome
  8. endocytic vesicle lumen Source: Reactome
  9. endoplasmic reticulum lumen Source: Reactome
  10. endoplasmic reticulum membrane Source: Reactome
  11. endosome lumen Source: Reactome
  12. endosome membrane Source: Reactome
  13. extracellular region Source: Reactome
  14. extracellular space Source: BHF-UCL
  15. extracellular vesicular exosome Source: UniProtKB
  16. Golgi apparatus Source: HPA
  17. intermediate-density lipoprotein particle Source: BHF-UCL
  18. intracellular membrane-bounded organelle Source: ProtInc
  19. low-density lipoprotein particle Source: BHF-UCL
  20. mature chylomicron Source: BHF-UCL
  21. plasma membrane Source: HPA
  22. very-low-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Chylomicron, Cytoplasm, LDL, Secreted, VLDL

Pathology & Biotechi

Involvement in diseasei

Hypobetalipoproteinemia, familial, 1 (FHBL1) [MIM:615558]: A disorder of lipid metabolism characterized by less than 5th percentile age- and sex-specific levels of low density lipoproteins, and dietary fat malabsorption. Clinical presentation may vary from no symptoms to severe gastrointestinal and neurological dysfunction similar to abetalipoproteinemia.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry. Most cases of FHBL1 result from nonsense mutations in the APOB gene that lead to a premature stop codon, which generate prematurely truncated apo B protein products (PubMed:21981844).1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti490 – 4901R → W in FHBL1; reduced protein secretion. 1 Publication
VAR_022610
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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3527 – 35271R → Q in FDB. 3 Publications
Corresponds to variant rs5742904 [ dbSNP | Ensembl ].
VAR_005025
Natural varianti3558 – 35581R → C in FDB. 2 Publications
Corresponds to variant rs12713559 [ dbSNP | Ensembl ].
VAR_005026
Defects in APOB associated with defects in other genes (polygenic) can contribute to hypocholesterolemia.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi483 – 4831D → N: Impairs protein secretion. 1 Publication
Mutagenesisi483 – 4831D → Q: Does not affect protein secretion. 1 Publication
Mutagenesisi490 – 4901R → A: Impairs protein secretion. 1 Publication
Mutagenesisi490 – 4901R → K: Does not affect protein secretion. 1 Publication

Keywords - Diseasei

Atherosclerosis, Disease mutation

Organism-specific databases

MIMi107730. gene+phenotype.
144010. phenotype.
615558. phenotype.
Orphaneti426. Familial hypobetalipoproteinemia.
406. Heterozygous familial hypercholesterolemia.
391665. Homozygous familial hypercholesterolemia.
PharmGKBiPA50.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Chaini28 – 45634536Apolipoprotein B-100PRO_0000020750Add
BLAST
Chaini28 – 21792152Apolipoprotein B-48PRO_0000020751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi39 ↔ 881 PublicationPROSITE-ProRule annotation
Disulfide bondi78 ↔ 971 PublicationPROSITE-ProRule annotation
Glycosylationi185 – 1851N-linked (GlcNAc...)1 Publication
Disulfide bondi186 ↔ 2121 PublicationPROSITE-ProRule annotation
Disulfide bondi245 ↔ 2611 PublicationPROSITE-ProRule annotation
Disulfide bondi385 ↔ 3901 PublicationPROSITE-ProRule annotation
Disulfide bondi478 ↔ 5131 PublicationPROSITE-ProRule annotation
Disulfide bondi966 ↔ 9761 PublicationPROSITE-ProRule annotation
Glycosylationi983 – 9831N-linked (GlcNAc...)Sequence Analysis
Lipidationi1112 – 11121S-palmitoyl cysteine1 Publication
Glycosylationi1368 – 13681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1377 – 13771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1523 – 15231N-linked (GlcNAc...)2 Publications
Modified residuei2004 – 20041N6-acetyllysine1 Publication
Glycosylationi2239 – 22391N-linked (GlcNAc...)1 Publication
Glycosylationi2560 – 25601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2779 – 27791N-linked (GlcNAc...)1 Publication
Glycosylationi2982 – 29821N-linked (GlcNAc...)2 Publications
Glycosylationi3101 – 31011N-linked (GlcNAc...)1 Publication
Disulfide bondi3194 ↔ 33241 PublicationPROSITE-ProRule annotation
Glycosylationi3224 – 32241N-linked (GlcNAc...)1 Publication
Glycosylationi3336 – 33361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3358 – 33581N-linked (GlcNAc...)1 Publication
Glycosylationi3411 – 34111N-linked (GlcNAc...)1 Publication
Glycosylationi3465 – 34651N-linked (GlcNAc...)2 Publications
Glycosylationi3895 – 38951N-linked (GlcNAc...)2 Publications
Glycosylationi4237 – 42371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4431 – 44311N-linked (GlcNAc...)Sequence Analysis

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

Proteomic databases

MaxQBiP04114.
PaxDbiP04114.
PeptideAtlasiP04114.
PRIDEiP04114.

PTM databases

PhosphoSiteiP04114.
UniCarbKBiP04114.

Expressioni

Inductioni

Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

Gene expression databases

BgeeiP04114.
ExpressionAtlasiP04114. baseline and differential.
GenevestigatoriP04114.

Organism-specific databases

HPAiCAB016070.
HPA049793.

Interactioni

Subunit structurei

Interacts with PCSK9.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
P299913EBI-3926040,EBI-8826488From a different organism.
LDLRP011304EBI-3926040,EBI-988319

Protein-protein interaction databases

BioGridi106835. 48 interactions.
DIPiDIP-44767N.
IntActiP04114. 16 interactions.
MINTiMINT-1506918.

Structurei

3D structure databases

ProteinModelPortaliP04114.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 672627VitellogeninPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 12695Heparin-bindingAdd
BLAST
Regioni232 – 30675Heparin-bindingAdd
BLAST
Regioni902 – 95958Heparin-bindingAdd
BLAST
Regioni2043 – 2178136Heparin-bindingAdd
BLAST
Regioni3161 – 323676Heparin-bindingAdd
BLAST
Regioni3174 – 318411Basic (possible receptor binding region)Add
BLAST
Regioni3373 – 339321LDL receptor bindingAdd
BLAST
Regioni3383 – 3516134Heparin-bindingAdd
BLAST
Regioni3386 – 33949Basic (possible receptor binding region)

Sequence similaritiesi

Contains 1 vitellogenin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG290405.
HOVERGENiHBG050546.
InParanoidiP04114.
KOiK14462.
OMAiHIPEFQL.
OrthoDBiEOG7VB2DG.
PhylomeDBiP04114.
TreeFamiTF331316.

Family and domain databases

Gene3Di1.25.10.20. 1 hit.
2.20.50.20. 2 hits.
2.20.80.10. 1 hit.
2.30.230.10. 1 hit.
InterProiIPR022176. ApoB100_C.
IPR016024. ARM-type_fold.
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]
PfamiPF12491. ApoB100_C. 1 hit.
PF06448. DUF1081. 1 hit.
PF09172. DUF1943. 1 hit.
PF01347. Vitellogenin_N. 1 hit.
[Graphical view]
SMARTiSM00638. LPD_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 2 hits.
PROSITEiPS51211. VITELLOGENIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04114-1 [UniParc]FASTAAdd to Basket

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        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
Length:4,563
Mass (Da):515,605
Last modified:July 13, 2010 - v2
Checksum:i6800F94BF6ADF698
GO

Sequence cautioni

The sequence AAA51752.1 differs from that shown. Reason: Frameshift at positions 942, 951, 1139, 1165, 1164, 1371 and 1385.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 133Missing in AAB60718. (PubMed:3030729)Curated
Sequence conflicti11 – 133Missing in CAA28420. (PubMed:3030729)Curated
Sequence conflicti329 – 3291L → V in AAA35549. (PubMed:3759943)Curated
Sequence conflicti645 – 6451L → I in AAA35549. (PubMed:3759943)Curated
Sequence conflicti704 – 7041L → P in AAB04636. (PubMed:3464946)Curated
Sequence conflicti792 – 80918LQLLG…TLQGI → SSSWKAASHGCPHSAGD in AAA51759. (PubMed:3860836)CuratedAdd
BLAST
Sequence conflicti793 – 7931Q → R in AAB04636. (PubMed:3464946)Curated
Sequence conflicti893 – 8931D → K AA sequence (PubMed:6373369)Curated
Sequence conflicti919 – 9191A → P in AAA35549. (PubMed:3759943)Curated
Sequence conflicti1109 – 11091H → D in CAA28420. (PubMed:3030729)Curated
Sequence conflicti1180 – 11801T → R in AAA51752. (PubMed:3461454)Curated
Sequence conflicti1271 – 12711F → S in AAB04636. (PubMed:3464946)Curated
Sequence conflicti1418 – 14181F → S in CAA28420. (PubMed:3030729)Curated
Sequence conflicti1445 – 14451N → I in AAA51752. (PubMed:3461454)Curated
Sequence conflicti1535 – 15351G → E in AAA51752. (PubMed:3461454)Curated
Sequence conflicti1867 – 18671R → G in AAB04636. (PubMed:3464946)Curated
Sequence conflicti2098 – 20981N → K in CAA28420. (PubMed:3030729)Curated
Sequence conflicti2218 – 22181I → T in AAB04636. (PubMed:3464946)Curated
Sequence conflicti2221 – 22211N → I in CAA28420. (PubMed:3030729)Curated
Sequence conflicti2324 – 23263LIG → PYW in AAA51741. (PubMed:3676265)Curated
Sequence conflicti2353 – 23531Q → H in AAA51741. (PubMed:3676265)Curated
Sequence conflicti2540 – 25401G → S in CAA28420. (PubMed:3030729)Curated
Sequence conflicti2718 – 273720Missing in AAA51758. (PubMed:2883086)CuratedAdd
BLAST
Sequence conflicti2933 – 29331C → S in AAB04636. (PubMed:3464946)Curated
Sequence conflicti3114 – 31141H → L AA sequence (PubMed:6373369)Curated
Sequence conflicti3131 – 31311T → R AA sequence (PubMed:6373369)Curated
Sequence conflicti3134 – 31341E → P AA sequence (PubMed:6373369)Curated
Sequence conflicti3137 – 31371L → R AA sequence (PubMed:6373369)Curated
Sequence conflicti3239 – 32391H → Q in CAA28420. (PubMed:3030729)Curated
Sequence conflicti3286 – 32861L → I in AAB04636. (PubMed:3464946)Curated
Sequence conflicti3291 – 32911R → L in AAA51758. (PubMed:2883086)Curated
Sequence conflicti3337 – 33371I → N in AAA51758. (PubMed:2883086)Curated
Sequence conflicti3431 – 34311A → P in AAB04636. (PubMed:3464946)Curated
Sequence conflicti3728 – 37281D → N in AAA51742. (PubMed:2932736)Curated
Sequence conflicti3782 – 37821N → T in AAB04636. (PubMed:3464946)Curated
Sequence conflicti3824 – 38241Q → R in CAA28420. (PubMed:3030729)Curated
Sequence conflicti3824 – 38241Q → R in AAA51750. (PubMed:2994225)Curated
Sequence conflicti3876 – 38761V → A in AAA35549. (PubMed:3759943)Curated
Sequence conflicti3876 – 38761V → A in AAA51742. (PubMed:2932736)Curated
Sequence conflicti3911 – 39111T → Y AA sequence (PubMed:2115173)Curated
Sequence conflicti3983 – 39831F → S in AAA51742. (PubMed:2932736)Curated
Sequence conflicti4002 – 40021A → P in AAA51742. (PubMed:2932736)Curated
Sequence conflicti4110 – 41112NN → DH in AAA35549. (PubMed:3759943)Curated
Sequence conflicti4110 – 41112NN → DH in AAA51742. (PubMed:2932736)Curated
Sequence conflicti4122 – 41221Q → E in AAA35549. (PubMed:3759943)Curated
Sequence conflicti4122 – 41221Q → E in AAA51742. (PubMed:2932736)Curated
Sequence conflicti4128 – 41281V → E in AAA35549. (PubMed:3759943)Curated
Sequence conflicti4128 – 41281V → E in AAA51742. (PubMed:2932736)Curated
Sequence conflicti4133 – 41331A → G in AAA35549. (PubMed:3759943)Curated
Sequence conflicti4133 – 41331A → G in AAA51742. (PubMed:2932736)Curated
Sequence conflicti4188 – 41881H → K in AAB04636. (PubMed:3464946)Curated
Sequence conflicti4217 – 42182CT → FP in AAA35548. (PubMed:3024665)Curated
Sequence conflicti4221 – 42211I → M in AAB04636. (PubMed:3464946)Curated

RNA editingi

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:107730].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 143Missing.1 Publication
VAR_067277
Natural varianti98 – 981T → I Polymorphism that influences plasma concentrations of low density lipoprotein cholesterol. 6 Publications
Corresponds to variant rs1367117 [ dbSNP | Ensembl ].
VAR_016184
Natural varianti103 – 1031Y → H.
Corresponds to variant rs9282603 [ dbSNP | Ensembl ].
VAR_022036
Natural varianti145 – 1451P → S.
Corresponds to variant rs6752026 [ dbSNP | Ensembl ].
VAR_022037
Natural varianti194 – 1941T → M.
Corresponds to variant rs13306198 [ dbSNP | Ensembl ].
VAR_056737
Natural varianti273 – 2731K → N.1 Publication
Corresponds to variant rs1126419 [ dbSNP | Ensembl ].
VAR_019827
Natural varianti408 – 4081I → T.
Corresponds to variant rs12714225 [ dbSNP | Ensembl ].
VAR_029341
Natural varianti490 – 4901R → W in FHBL1; reduced protein secretion. 1 Publication
VAR_022610
Natural varianti554 – 5541P → L.
Corresponds to variant rs12714214 [ dbSNP | Ensembl ].
VAR_020135
Natural varianti618 – 6181A → V.3 Publications
Corresponds to variant rs679899 [ dbSNP | Ensembl ].
VAR_019828
Natural varianti730 – 7301V → I.1 Publication
Corresponds to variant rs12691202 [ dbSNP | Ensembl ].
VAR_020136
Natural varianti733 – 7331V → I.
Corresponds to variant rs1800476 [ dbSNP | Ensembl ].
VAR_016185
Natural varianti741 – 7411T → N.
Corresponds to variant rs12714192 [ dbSNP | Ensembl ].
VAR_020137
Natural varianti877 – 8771P → L.
Corresponds to variant rs12714097 [ dbSNP | Ensembl ].
VAR_029342
Natural varianti955 – 9551P → S.
Corresponds to variant rs13306206 [ dbSNP | Ensembl ].
VAR_056738
Natural varianti1086 – 10861G → S.
Corresponds to variant rs12720801 [ dbSNP | Ensembl ].
VAR_029343
Natural varianti1113 – 11131D → H.
Corresponds to variant rs12713844 [ dbSNP | Ensembl ].
VAR_029344
Natural varianti1128 – 11281R → H.1 Publication
Corresponds to variant rs12713843 [ dbSNP | Ensembl ].
VAR_022611
Natural varianti1218 – 12181Q → E Polymorphism confirmed at protein level. 2 Publications
Corresponds to variant rs1041956 [ dbSNP | Ensembl ].
VAR_019829
Natural varianti1388 – 13881R → H.
Corresponds to variant rs13306187 [ dbSNP | Ensembl ].
VAR_029345
Natural varianti1422 – 14221Y → C.8 Publications
Corresponds to variant rs568413 [ dbSNP | Ensembl ].
VAR_061558
Natural varianti1437 – 14371F → L.1 Publication
Corresponds to variant rs1801697 [ dbSNP | Ensembl ].
VAR_005016
Natural varianti1613 – 16131S → T.1 Publication
VAR_067278
Natural varianti1670 – 16701E → D Polymorphism confirmed at protein level. 2 Publications
VAR_068911
Natural varianti1914 – 19141N → S.2 Publications
Corresponds to variant rs1801699 [ dbSNP | Ensembl ].
VAR_005017
Natural varianti1923 – 19231H → R.2 Publications
Corresponds to variant rs533617 [ dbSNP | Ensembl ].
VAR_005018
Natural varianti2037 – 20371I → N Polymorphism confirmed at protein level. 2 Publications
VAR_068912
Natural varianti2092 – 20921L → V.1 Publication
Corresponds to variant rs1041960 [ dbSNP | Ensembl ].
VAR_019830
Natural varianti2299 – 22991D → H.
Corresponds to variant rs12713681 [ dbSNP | Ensembl ].
VAR_029346
Natural varianti2313 – 23131I → V.8 Publications
Corresponds to variant rs584542 [ dbSNP | Ensembl ].
VAR_059582
Natural varianti2365 – 23651A → T.1 Publication
Corresponds to variant rs1041971 [ dbSNP | Ensembl ].
VAR_019831
Natural varianti2456 – 24561A → D.
Corresponds to variant rs12713675 [ dbSNP | Ensembl ].
VAR_020138
Natural varianti2564 – 25641F → C in a colorectal cancer sample; somatic mutation; polymorphism confirmed at protein level. 2 Publications
VAR_035795
Natural varianti2566 – 25661E → K Polymorphism confirmed at protein level. 3 Publications
Corresponds to variant rs1801696 [ dbSNP | Ensembl ].
VAR_005019
Natural varianti2680 – 26801L → Q.1 Publication
Corresponds to variant rs1042013 [ dbSNP | Ensembl ].
VAR_019832
Natural varianti2739 – 27391P → L.3 Publications
Corresponds to variant rs676210 [ dbSNP | Ensembl ].
VAR_005020
Natural varianti2785 – 27851N → H.
Corresponds to variant rs2163204 [ dbSNP | Ensembl ].
VAR_022038
Natural varianti3121 – 31211A → T.1 Publication
Corresponds to variant rs1801694 [ dbSNP | Ensembl ].
VAR_005021
Natural varianti3182 – 31821H → N.
Corresponds to variant rs12720848 [ dbSNP | Ensembl ].
VAR_029347
Natural varianti3279 – 32791S → G.
Corresponds to variant rs12720854 [ dbSNP | Ensembl ].
VAR_029348
Natural varianti3294 – 32941S → P.
Corresponds to variant rs12720855 [ dbSNP | Ensembl ].
VAR_020139
Natural varianti3319 – 33191D → H.8 Publications
VAR_005022
Natural varianti3427 – 34271T → K.8 Publications
VAR_005023
Natural varianti3432 – 34321Q → E.8 Publications
Corresponds to variant rs1042023 [ dbSNP | Ensembl ].
VAR_005024
Natural varianti3527 – 35271R → Q in FDB. 3 Publications
Corresponds to variant rs5742904 [ dbSNP | Ensembl ].
VAR_005025
Natural varianti3558 – 35581R → C in FDB. 2 Publications
Corresponds to variant rs12713559 [ dbSNP | Ensembl ].
VAR_005026
Natural varianti3638 – 36381R → Q.1 Publication
Corresponds to variant rs1801701 [ dbSNP | Ensembl ].
VAR_016186
Natural varianti3732 – 37321I → T.4 Publications
Corresponds to variant rs1042025 [ dbSNP | Ensembl ].
VAR_019833
Natural varianti3801 – 38011S → T.
Corresponds to variant rs12713540 [ dbSNP | Ensembl ].
VAR_029349
Natural varianti3835 – 38351I → L.1 Publication
VAR_067279
Natural varianti3921 – 39211V → I.1 Publication
Corresponds to variant rs72654409 [ dbSNP | Ensembl ].
VAR_005027
Natural varianti3945 – 39451T → A.1 Publication
Corresponds to variant rs1801698 [ dbSNP | Ensembl ].
VAR_005028
Natural varianti3949 – 39491F → L.5 Publications
Corresponds to variant rs1042027 [ dbSNP | Ensembl ].
VAR_019834
Natural varianti3964 – 39641Y → F.4 Publications
Corresponds to variant rs1126468 [ dbSNP | Ensembl ].
VAR_019835
Natural varianti4128 – 41281V → M.1 Publication
Corresponds to variant rs1801703 [ dbSNP | Ensembl ].
VAR_005029
Natural varianti4181 – 41811E → K.6 Publications
Corresponds to variant rs1042031 [ dbSNP | Ensembl ].
VAR_016187
Natural varianti4270 – 42701R → T.1 Publication
Corresponds to variant rs1801702 [ dbSNP | Ensembl ].
VAR_016188
Natural varianti4314 – 43141I → V.1 Publication
Corresponds to variant rs72654423 [ dbSNP | Ensembl ].
VAR_067280
Natural varianti4338 – 43381S → N.11 Publications
Corresponds to variant rs1042034 [ dbSNP | Ensembl ].
VAR_005030
Natural varianti4394 – 43941V → A.
Corresponds to variant rs12720843 [ dbSNP | Ensembl ].
VAR_029350
Natural varianti4481 – 44811A → T.2 Publications
Corresponds to variant rs1801695 [ dbSNP | Ensembl ].
VAR_005031
Natural varianti4482 – 44821I → V.1 Publication
VAR_067281
Natural varianti4484 – 44841T → M.
Corresponds to variant rs12713450 [ dbSNP | Ensembl ].
VAR_020140

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS1703.1.
PIRiA27850. LPHUB.
RefSeqiNP_000375.2. NM_000384.2.
UniGeneiHs.120759.

Genome annotation databases

EnsembliENST00000233242; ENSP00000233242; ENSG00000084674.
GeneIDi338.
KEGGihsa:338.

Polymorphism databases

DMDMi300669605.

Keywords - Coding sequence diversityi

Polymorphism, RNA editing

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Apolipoprotein B entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UniGenei Hs.120759.

3D structure databases

ProteinModelPortali P04114.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106835. 48 interactions.
DIPi DIP-44767N.
IntActi P04114. 16 interactions.
MINTi MINT-1506918.

Chemistry

BindingDBi P04114.
ChEMBLi CHEMBL4549.

PTM databases

PhosphoSitei P04114.
UniCarbKBi P04114.

Polymorphism databases

DMDMi 300669605.

Proteomic databases

MaxQBi P04114.
PaxDbi P04114.
PeptideAtlasi P04114.
PRIDEi P04114.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233242 ; ENSP00000233242 ; ENSG00000084674 .
GeneIDi 338.
KEGGi hsa:338.

Organism-specific databases

CTDi 338.
GeneCardsi GC02M021135.
GeneReviewsi APOB.
H-InvDB HIX0024005.
HGNCi HGNC:603. APOB.
HPAi CAB016070.
HPA049793.
MIMi 107730. gene+phenotype.
144010. phenotype.
615558. phenotype.
neXtProti NX_P04114.
Orphaneti 426. Familial hypobetalipoproteinemia.
406. Heterozygous familial hypercholesterolemia.
391665. Homozygous familial hypercholesterolemia.
PharmGKBi PA50.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG290405.
HOVERGENi HBG050546.
InParanoidi P04114.
KOi K14462.
OMAi HIPEFQL.
OrthoDBi EOG7VB2DG.
PhylomeDBi P04114.
TreeFami TF331316.

Enzyme and pathway databases

Reactomei REACT_12051. Cell surface interactions at the vascular wall.
REACT_163679. Scavenging by Class B Receptors.
REACT_163699. Scavenging by Class A Receptors.
REACT_163813. Scavenging by Class F Receptors.
REACT_164002. Scavenging by Class H Receptors.
REACT_23879. Platelet sensitization by LDL.
REACT_24968. Retinoid metabolism and transport.
REACT_6841. Chylomicron-mediated lipid transport.
REACT_6934. LDL-mediated lipid transport.

Miscellaneous databases

ChiTaRSi APOB. human.
GeneWikii Apolipoprotein_B.
GenomeRNAii 338.
NextBioi 1399.
PROi P04114.
SOURCEi Search...

Gene expression databases

Bgeei P04114.
ExpressionAtlasi P04114. baseline and differential.
Genevestigatori P04114.

Family and domain databases

Gene3Di 1.25.10.20. 1 hit.
2.20.50.20. 2 hits.
2.20.80.10. 1 hit.
2.30.230.10. 1 hit.
InterProi IPR022176. ApoB100_C.
IPR016024. ARM-type_fold.
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 ]
Pfami PF12491. ApoB100_C. 1 hit.
PF06448. DUF1081. 1 hit.
PF09172. DUF1943. 1 hit.
PF01347. Vitellogenin_N. 1 hit.
[Graphical view ]
SMARTi SM00638. LPD_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
SSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 2 hits.
PROSITEi PS51211. VITELLOGENIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 709-906.
  13. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1671-2398, VARIANT VAL-2313.
  17. 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. 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. 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. 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.
    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.
    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, IDENTIFICATION BY 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.
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Biological, clinical and population relevance of 95 loci for blood lipids."
    Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C., Stylianou I.M., Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I., Willer C.J., Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M., Barbalic M., Ricketts S.L., Bis J.C., Aulchenko Y.S.
    , Thorleifsson G., Feitosa M.F., Chambers J., Orho-Melander M., Melander O., Johnson T., Li X., Guo X., Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y., Park T., Kim K., Sim X., Twee-Hee Ong R., Croteau-Chonka D.C., Lange L.A., Smith J.D., Song K., Hua Zhao J., Yuan X., Luan J., Lamina C., Ziegler A., Zhang W., Zee R.Y., Wright A.F., Witteman J.C., Wilson J.F., Willemsen G., Wichmann H.E., Whitfield J.B., Waterworth D.M., Wareham N.J., Waeber G., Vollenweider P., Voight B.F., Vitart V., Uitterlinden A.G., Uda M., Tuomilehto J., Thompson J.R., Tanaka T., Surakka I., Stringham H.M., Spector T.D., Soranzo N., Smit J.H., Sinisalo J., Silander K., Sijbrands E.J., Scuteri A., Scott J., Schlessinger D., Sanna S., Salomaa V., Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M., Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I., Perola M., Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N., Pare G., Oostra B.A., O'Donnell C.J., Nieminen M.S., Nickerson D.A., Montgomery G.W., Meitinger T., McPherson R., McCarthy M.I., McArdle W., Masson D., Martin N.G., Marroni F., Mangino M., Magnusson P.K., Lucas G., Luben R., Loos R.J., Lokki M.L., Lettre G., Langenberg C., Launer L.J., Lakatta E.G., Laaksonen R., Kyvik K.O., Kronenberg F., Konig I.R., Khaw K.T., Kaprio J., Kaplan L.M., Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E., Igl W., Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A., Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D., Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C., Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L., Erdmann J., Elliott P., Ejebe K.G., Doring A., Dominiczak A.F., Demissie S., Deloukas P., de Geus E.J., de Faire U., Crawford G., Collins F.S., Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P., Bonnycastle L.L., Boomsma D.I., Boekholdt S.M., Bergman R.N., Barroso I., Bandinelli S., Ballantyne C.M., Assimes T.L., Quertermous T., Altshuler D., Seielstad M., Wong T.Y., Tai E.S., Feranil A.B., Kuzawa C.W., Adair L.S., Taylor H.A. Jr., Borecki I.B., Gabriel S.B., Wilson J.G., Holm H., Thorsteinsdottir U., Gudnason V., Krauss R.M., Mohlke K.L., Ordovas J.M., Munroe P.B., Kooner J.S., Tall A.R., Hegele R.A., Kastelein J.J., Schadt E.E., Rotter J.I., Boerwinkle E., Strachan D.P., Mooser V., Stefansson K., Reilly M.P., Samani N.J., Schunkert H., Cupples L.A., Sandhu M.S., Ridker P.M., Rader D.J., van Duijn C.M., Peltonen L., Abecasis G.R., Boehnke M., Kathiresan S.
    Nature 466:707-713(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LDLCQ4, VARIANT ILE-98.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "A novel mutation of apolipoprotein B in a French Canadian family with homozygous hypobetalipoproteinemia."
    Gangloff A., Bergeron J., Couture P., Martins R., Hegele R.A., Gagne C.
    J. Clin. Lipidol. 5:414-417(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FHBL1.
  40. "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.
  41. "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.
  42. "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.
  43. "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.
  44. "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.
  45. "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.
  46. "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.
  47. "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.
  48. "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.
  49. "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.
  50. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-2564.
  51. "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.
  52. "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, IDENTIFICATION BY MASS SPECTROMETRY.
  53. "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.

Entry informationi

Entry nameiAPOB_HUMAN
AccessioniPrimary (citable) accession number: P04114
Secondary accession number(s): O00502
, P78479, P78480, P78481, Q13779, Q13785, Q13786, Q13787, Q13788, Q4ZG63, Q53QC8, Q7Z600, Q9UMN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: July 13, 2010
Last modified: October 29, 2014
This is version 180 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3