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P04114

- APOB_HUMAN

UniProt

P04114 - APOB_HUMAN

Protein

Apolipoprotein B-100

Gene

APOB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 2 (13 Jul 2010)
      Previous versions | rss
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    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
    6. protein binding Source: UniProtKB

    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

    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. Golgi apparatus Source: HPA
    16. intermediate-density lipoprotein particle Source: BHF-UCL
    17. intracellular membrane-bounded organelle Source: ProtInc
    18. low-density lipoprotein particle Source: BHF-UCL
    19. mature chylomicron Source: BHF-UCL
    20. plasma membrane Source: HPA
    21. very-low-density lipoprotein particle Source: BHF-UCL

    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

    ArrayExpressiP04114.
    BgeeiP04114.
    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. 39 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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    MDPPRPALLA LLALPALLLL LLAGARAEEE MLENVSLVCP KDATRFKHLR     50
    KYTYNYEAES SSGVPGTADS RSATRINCKV ELEVPQLCSF ILKTSQCTLK 100
    EVYGFNPEGK ALLKKTKNSE EFAAAMSRYE LKLAIPEGKQ VFLYPEKDEP 150
    TYILNIKRGI ISALLVPPET EEAKQVLFLD TVYGNCSTHF TVKTRKGNVA 200
    TEISTERDLG QCDRFKPIRT GISPLALIKG MTRPLSTLIS SSQSCQYTLD 250
    AKRKHVAEAI CKEQHLFLPF SYKNKYGMVA QVTQTLKLED TPKINSRFFG 300
    EGTKKMGLAF ESTKSTSPPK QAEAVLKTLQ ELKKLTISEQ NIQRANLFNK 350
    LVTELRGLSD EAVTSLLPQL IEVSSPITLQ ALVQCGQPQC STHILQWLKR 400
    VHANPLLIDV VTYLVALIPE PSAQQLREIF NMARDQRSRA TLYALSHAVN 450
    NYHKTNPTGT QELLDIANYL MEQIQDDCTG DEDYTYLILR VIGNMGQTME 500
    QLTPELKSSI LKCVQSTKPS LMIQKAAIQA LRKMEPKDKD QEVLLQTFLD 550
    DASPGDKRLA AYLMLMRSPS QADINKIVQI LPWEQNEQVK NFVASHIANI 600
    LNSEELDIQD LKKLVKEALK ESQLPTVMDF RKFSRNYQLY KSVSLPSLDP 650
    ASAKIEGNLI FDPNNYLPKE SMLKTTLTAF GFASADLIEI GLEGKGFEPT 700
    LEALFGKQGF FPDSVNKALY WVNGQVPDGV SKVLVDHFGY TKDDKHEQDM 750
    VNGIMLSVEK LIKDLKSKEV PEARAYLRIL GEELGFASLH DLQLLGKLLL 800
    MGARTLQGIP QMIGEVIRKG SKNDFFLHYI FMENAFELPT GAGLQLQISS 850
    SGVIAPGAKA GVKLEVANMQ AELVAKPSVS VEFVTNMGII IPDFARSGVQ 900
    MNTNFFHESG LEAHVALKAG KLKFIIPSPK RPVKLLSGGN TLHLVSTTKT 950
    EVIPPLIENR QSWSVCKQVF PGLNYCTSGA YSNASSTDSA SYYPLTGDTR 1000
    LELELRPTGE IEQYSVSATY ELQREDRALV DTLKFVTQAE GAKQTEATMT 1050
    FKYNRQSMTL SSEVQIPDFD VDLGTILRVN DESTEGKTSY RLTLDIQNKK 1100
    ITEVALMGHL SCDTKEERKI KGVISIPRLQ AEARSEILAH WSPAKLLLQM 1150
    DSSATAYGST VSKRVAWHYD EEKIEFEWNT GTNVDTKKMT SNFPVDLSDY 1200
    PKSLHMYANR LLDHRVPQTD MTFRHVGSKL IVAMSSWLQK ASGSLPYTQT 1250
    LQDHLNSLKE FNLQNMGLPD FHIPENLFLK SDGRVKYTLN KNSLKIEIPL 1300
    PFGGKSSRDL KMLETVRTPA LHFKSVGFHL PSREFQVPTF TIPKLYQLQV 1350
    PLLGVLDLST NVYSNLYNWS ASYSGGNTST DHFSLRARYH MKADSVVDLL 1400
    SYNVQGSGET TYDHKNTFTL SYDGSLRHKF LDSNIKFSHV EKLGNNPVSK 1450
    GLLIFDASSS WGPQMSASVH LDSKKKQHLF VKEVKIDGQF RVSSFYAKGT 1500
    YGLSCQRDPN TGRLNGESNL RFNSSYLQGT NQITGRYEDG TLSLTSTSDL 1550
    QSGIIKNTAS LKYENYELTL KSDTNGKYKN FATSNKMDMT FSKQNALLRS 1600
    EYQADYESLR FFSLLSGSLN SHGLELNADI LGTDKINSGA HKATLRIGQD 1650
    GISTSATTNL KCSLLVLENE LNAELGLSGA SMKLTTNGRF REHNAKFSLD 1700
    GKAALTELSL GSAYQAMILG VDSKNIFNFK VSQEGLKLSN DMMGSYAEMK 1750
    FDHTNSLNIA GLSLDFSSKL DNIYSSDKFY KQTVNLQLQP YSLVTTLNSD 1800
    LKYNALDLTN NGKLRLEPLK LHVAGNLKGA YQNNEIKHIY AISSAALSAS 1850
    YKADTVAKVQ GVEFSHRLNT DIAGLASAID MSTNYNSDSL HFSNVFRSVM 1900
    APFTMTIDAH TNGNGKLALW GEHTGQLYSK FLLKAEPLAF TFSHDYKGST 1950
    SHHLVSRKSI SAALEHKVSA LLTPAEQTGT WKLKTQFNNN EYSQDLDAYN 2000
    TKDKIGVELT GRTLADLTLL DSPIKVPLLL SEPINIIDAL EMRDAVEKPQ 2050
    EFTIVAFVKY DKNQDVHSIN LPFFETLQEY FERNRQTIIV VLENVQRNLK 2100
    HINIDQFVRK YRAALGKLPQ QANDYLNSFN WERQVSHAKE KLTALTKKYR 2150
    ITENDIQIAL DDAKINFNEK LSQLQTYMIQ FDQYIKDSYD LHDLKIAIAN 2200
    IIDEIIEKLK SLDEHYHIRV NLVKTIHDLH LFIENIDFNK SGSSTASWIQ 2250
    NVDTKYQIRI QIQEKLQQLK RHIQNIDIQH LAGKLKQHIE AIDVRVLLDQ 2300
    LGTTISFERI NDILEHVKHF VINLIGDFEV AEKINAFRAK VHELIERYEV 2350
    DQQIQVLMDK LVELAHQYKL KETIQKLSNV LQQVKIKDYF EKLVGFIDDA 2400
    VKKLNELSFK TFIEDVNKFL DMLIKKLKSF DYHQFVDETN DKIREVTQRL 2450
    NGEIQALELP QKAEALKLFL EETKATVAVY LESLQDTKIT LIINWLQEAL 2500
    SSASLAHMKA KFRETLEDTR DRMYQMDIQQ ELQRYLSLVG QVYSTLVTYI 2550
    SDWWTLAAKN LTDFAEQYSI QDWAKRMKAL VEQGFTVPEI KTILGTMPAF 2600
    EVSLQALQKA TFQTPDFIVP LTDLRIPSVQ INFKDLKNIK IPSRFSTPEF 2650
    TILNTFHIPS FTIDFVEMKV KIIRTIDQML NSELQWPVPD IYLRDLKVED 2700
    IPLARITLPD FRLPEIAIPE FIIPTLNLND FQVPDLHIPE FQLPHISHTI 2750
    EVPTFGKLYS ILKIQSPLFT LDANADIGNG TTSANEAGIA ASITAKGESK 2800
    LEVLNFDFQA NAQLSNPKIN PLALKESVKF SSKYLRTEHG SEMLFFGNAI 2850
    EGKSNTVASL HTEKNTLELS NGVIVKINNQ LTLDSNTKYF HKLNIPKLDF 2900
    SSQADLRNEI KTLLKAGHIA WTSSGKGSWK WACPRFSDEG THESQISFTI 2950
    EGPLTSFGLS NKINSKHLRV NQNLVYESGS LNFSKLEIQS QVDSQHVGHS 3000
    VLTAKGMALF GEGKAEFTGR HDAHLNGKVI GTLKNSLFFS AQPFEITAST 3050
    NNEGNLKVRF PLRLTGKIDF LNNYALFLSP SAQQASWQVS ARFNQYKYNQ 3100
    NFSAGNNENI MEAHVGINGE ANLDFLNIPL TIPEMRLPYT IITTPPLKDF 3150
    SLWEKTGLKE FLKTTKQSFD LSVKAQYKKN KHRHSITNPL AVLCEFISQS 3200
    IKSFDRHFEK NRNNALDFVT KSYNETKIKF DKYKAEKSHD ELPRTFQIPG 3250
    YTVPVVNVEV SPFTIEMSAF GYVFPKAVSM PSFSILGSDV RVPSYTLILP 3300
    SLELPVLHVP RNLKLSLPDF KELCTISHIF IPAMGNITYD FSFKSSVITL 3350
    NTNAELFNQS DIVAHLLSSS SSVIDALQYK LEGTTRLTRK RGLKLATALS 3400
    LSNKFVEGSH NSTVSLTTKN MEVSVATTTK AQIPILRMNF KQELNGNTKS 3450
    KPTVSSSMEF KYDFNSSMLY STAKGAVDHK LSLESLTSYF SIESSTKGDV 3500
    KGSVLSREYS GTIASEANTY LNSKSTRSSV KLQGTSKIDD IWNLEVKENF 3550
    AGEATLQRIY SLWEHSTKNH LQLEGLFFTN GEHTSKATLE LSPWQMSALV 3600
    QVHASQPSSF HDFPDLGQEV ALNANTKNQK IRWKNEVRIH SGSFQSQVEL 3650
    SNDQEKAHLD IAGSLEGHLR FLKNIILPVY DKSLWDFLKL DVTTSIGRRQ 3700
    HLRVSTAFVY TKNPNGYSFS IPVKVLADKF IIPGLKLNDL NSVLVMPTFH 3750
    VPFTDLQVPS CKLDFREIQI YKKLRTSSFA LNLPTLPEVK FPEVDVLTKY 3800
    SQPEDSLIPF FEITVPESQL TVSQFTLPKS VSDGIAALDL NAVANKIADF 3850
    ELPTIIVPEQ TIEIPSIKFS VPAGIVIPSF QALTARFEVD SPVYNATWSA 3900
    SLKNKADYVE TVLDSTCSST VQFLEYELNV LGTHKIEDGT LASKTKGTFA 3950
    HRDFSAEYEE DGKYEGLQEW EGKAHLNIKS PAFTDLHLRY QKDKKGISTS 4000
    AASPAVGTVG MDMDEDDDFS KWNFYYSPQS SPDKKLTIFK TELRVRESDE 4050
    ETQIKVNWEE EAASGLLTSL KDNVPKATGV LYDYVNKYHW EHTGLTLREV 4100
    SSKLRRNLQN NAEWVYQGAI RQIDDIDVRF QKAASGTTGT YQEWKDKAQN 4150
    LYQELLTQEG QASFQGLKDN VFDGLVRVTQ EFHMKVKHLI DSLIDFLNFP 4200
    RFQFPGKPGI YTREELCTMF IREVGTVLSQ VYSKVHNGSE ILFSYFQDLV 4250
    ITLPFELRKH KLIDVISMYR ELLKDLSKEA QEVFKAIQSL KTTEVLRNLQ 4300
    DLLQFIFQLI EDNIKQLKEM KFTYLINYIQ DEINTIFSDY IPYVFKLLKE 4350
    NLCLNLHKFN EFIQNELQEA SQELQQIHQY IMALREEYFD PSIVGWTVKY 4400
    YELEEKIVSL IKNLLVALKD FHSEYIVSAS NFTSQLSSQV EQFLHRNIQE 4450
    YLSILTDPDG KGKEKIAELS ATAQEIIKSQ AIATKKIISD YHQQFRYKLQ 4500
    DFSDQLSDYY EKFIAESKRL IDLSIQNYHT FLIYITELLK KLQSTTVMNP 4550
    YMKLAPGELT IIL 4563
    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.
    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. 39 interactions.
    DIPi DIP-44767N.
    IntActi P04114. 16 interactions.
    MINTi MINT-1506918.

    Chemistry

    BindingDBi P04114.
    ChEMBLi CHEMBL4549.
    DrugBanki DB01076. Atorvastatin.

    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

    ArrayExpressi P04114.
    Bgeei P04114.
    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

    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 1, 2014
    This is version 179 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