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P04114 (APOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein B-100

Short name=Apo B-100

Cleaved into the following chain:

  1. Apolipoprotein B-48
    Short name=Apo B-48
Gene names
Name:APOB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4563 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor.

Subunit structure

Interacts with PCSK9. Ref.40

Subcellular location

Cytoplasm. Secreted Ref.40.

Induction

Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.34

Post-translational modification

Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle. Ref.31

Polymorphism

Genetic variations in APOB define the low density lipoprotein cholesterol level quantitative trait locus 4 (LDLCQ4) [MIM:107730].

Involvement in disease

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.
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 (Ref.39). Ref.39 Ref.48

Familial ligand-defective apolipoprotein B-100 (FDB) [MIM:144010]: Dominantly inherited disorder of lipoprotein metabolism leading to hypercholesterolemia and increased proneness to coronary artery disease (CAD). The plasma cholesterol levels are dramatically elevated due to impaired clearance of LDL particles by defective APOB/E receptors.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.42 Ref.44 Ref.46 Ref.51

Defects in APOB associated with defects in other genes (polygenic) can contribute to hypocholesterolemia.

Sequence similarities

Contains 1 vitellogenin domain.

RNA editing

Edited at position 2180.
The stop codon (UAA) at position 2180 is created by RNA editing. Apo B-48, derived from the fully edited RNA, is produced only in the intestine and is found in chylomicrons. Apo B-48 is a shortened form of apo B-100 which lacks the LDL-receptor region. The unedited version (apo B-100) is produced by the liver and is found in the VLDL and LDL.

Sequence caution

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

Ontologies

Keywords
   Biological processCholesterol metabolism
Lipid metabolism
Lipid transport
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentChylomicron
Cytoplasm
LDL
Secreted
VLDL
   Coding sequence diversityPolymorphism
RNA editing
   DiseaseAtherosclerosis
Disease mutation
   DomainSignal
   LigandHeparin-binding
   PTMAcetylation
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processartery morphogenesis

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cellular response to prostaglandin stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

cholesterol efflux

Inferred from electronic annotation. Source: Ensembl

cholesterol homeostasis

Inferred from mutant phenotype Ref.42. Source: BHF-UCL

cholesterol metabolic process

Inferred from mutant phenotype Ref.42. Source: BHF-UCL

cholesterol transport

Inferred from mutant phenotype Ref.42. Source: BHF-UCL

fertilization

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Traceable author statement. Source: Reactome

lipoprotein biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein catabolic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein metabolic process

Traceable author statement. Source: Reactome

lipoprotein transport

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle clearance

Inferred from mutant phenotype PubMed 15797858Ref.42. Source: BHF-UCL

low-density lipoprotein particle remodeling

Inferred from mutant phenotype PubMed 15797858. Source: BHF-UCL

nervous system development

Inferred from electronic annotation. Source: Ensembl

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of cholesterol storage

Inferred from direct assay PubMed 19114110. Source: BHF-UCL

positive regulation of lipid storage

Inferred from direct assay PubMed 18322245. Source: BHF-UCL

positive regulation of macrophage derived foam cell differentiation

Inferred from direct assay PubMed 17244792PubMed 18322245PubMed 19114110. Source: BHF-UCL

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

receptor-mediated endocytosis

Traceable author statement. Source: Reactome

regulation of cholesterol biosynthetic process

Inferred from electronic annotation. Source: Ensembl

response to carbohydrate

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to selenium ion

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from expression pattern Ref.34. Source: UniProtKB

retinoid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

sperm motility

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

triglyceride catabolic process

Inferred from electronic annotation. Source: Ensembl

triglyceride mobilization

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle assembly

Inferred by curator PubMed 15308631. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

actin cytoskeleton

Inferred from direct assay. Source: HPA

chylomicron

Inferred from direct assay PubMed 4363408PubMed 8245722. Source: BHF-UCL

chylomicron remnant

Traceable author statement PubMed 6099394. Source: BHF-UCL

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

cytoplasm

Inferred from direct assay Ref.40. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

early endosome

Traceable author statement. Source: Reactome

endocytic vesicle lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

endosome lumen

Traceable author statement. Source: Reactome

endosome membrane

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from sequence or structural similarity PubMed 22261194. Source: BHF-UCL

intermediate-density lipoprotein particle

Inferred from direct assay PubMed 1917954. Source: BHF-UCL

intracellular membrane-bounded organelle

Traceable author statement PubMed 7853698. Source: ProtInc

low-density lipoprotein particle

Inferred from direct assay PubMed 4363408. Source: BHF-UCL

mature chylomicron

Inferred from direct assay PubMed 4363408. Source: BHF-UCL

plasma membrane

Inferred from direct assay. Source: HPA

very-low-density lipoprotein particle

Inferred from direct assay PubMed 15308631PubMed 4363408. Source: BHF-UCL

   Molecular_functioncholesterol transporter activity

Inferred from mutant phenotype PubMed 15797858. Source: BHF-UCL

heparin binding

Inferred from direct assay PubMed 16233946. Source: BHF-UCL

lipase binding

Inferred from physical interaction PubMed 9685400. Source: BHF-UCL

low-density lipoprotein particle receptor binding

Inferred from mutant phenotype PubMed 15797858Ref.42. Source: BHF-UCL

phospholipid binding

Inferred from direct assay PubMed 7126555. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P299913EBI-3926040,EBI-8826488From a different organism.
LDLRP011304EBI-3926040,EBI-988319

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 45634536Apolipoprotein B-100
PRO_0000020750
Chain28 – 21792152Apolipoprotein B-48
PRO_0000020751

Regions

Domain46 – 672627Vitellogenin
Region32 – 12695Heparin-binding
Region232 – 30675Heparin-binding
Region902 – 95958Heparin-binding
Region2043 – 2178136Heparin-binding
Region3161 – 323676Heparin-binding
Region3174 – 318411Basic (possible receptor binding region)
Region3373 – 339321LDL receptor binding
Region3383 – 3516134Heparin-binding
Region3386 – 33949Basic (possible receptor binding region)

Amino acid modifications

Modified residue20041N6-acetyllysine Ref.36
Lipidation11121S-palmitoyl cysteine Ref.31
Glycosylation341N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Ref.35
Glycosylation9831N-linked (GlcNAc...) Potential
Glycosylation13681N-linked (GlcNAc...) Potential
Glycosylation13771N-linked (GlcNAc...) Potential
Glycosylation15231N-linked (GlcNAc...) Ref.33 Ref.35
Glycosylation22391N-linked (GlcNAc...) Ref.35
Glycosylation25601N-linked (GlcNAc...) Potential
Glycosylation27791N-linked (GlcNAc...) Ref.35
Glycosylation29821N-linked (GlcNAc...) Ref.33 Ref.35
Glycosylation31011N-linked (GlcNAc...) Ref.35
Glycosylation32241N-linked (GlcNAc...) Ref.35
Glycosylation33361N-linked (GlcNAc...) Potential
Glycosylation33581N-linked (GlcNAc...) Ref.32
Glycosylation34111N-linked (GlcNAc...) Ref.35
Glycosylation34651N-linked (GlcNAc...) Ref.33 Ref.35
Glycosylation38951N-linked (GlcNAc...) Ref.33 Ref.35
Glycosylation42371N-linked (GlcNAc...) Potential
Glycosylation44311N-linked (GlcNAc...) Potential
Disulfide bond39 ↔ 88 Ref.10
Disulfide bond78 ↔ 97 Ref.10
Disulfide bond186 ↔ 212 Ref.10
Disulfide bond245 ↔ 261 Ref.10
Disulfide bond385 ↔ 390 Ref.10
Disulfide bond478 ↔ 513 Ref.10
Disulfide bond966 ↔ 976 Ref.10
Disulfide bond3194 ↔ 3324 Ref.10

Natural variations

Natural variant12 – 143Missing.
VAR_067277
Natural variant981T → I Polymorphism that influences plasma concentrations of low density lipoprotein cholesterol. Ref.3 Ref.8 Ref.10 Ref.37 Ref.48 Ref.53
Corresponds to variant rs1367117 [ dbSNP | Ensembl ].
VAR_016184
Natural variant1031Y → H.
Corresponds to variant rs9282603 [ dbSNP | Ensembl ].
VAR_022036
Natural variant1451P → S.
Corresponds to variant rs6752026 [ dbSNP | Ensembl ].
VAR_022037
Natural variant1941T → M.
Corresponds to variant rs13306198 [ dbSNP | Ensembl ].
VAR_056737
Natural variant2731K → N. Ref.1
Corresponds to variant rs1126419 [ dbSNP | Ensembl ].
VAR_019827
Natural variant4081I → T.
Corresponds to variant rs12714225 [ dbSNP | Ensembl ].
VAR_029341
Natural variant4901R → W in FHBL1; reduced protein secretion. Ref.48
VAR_022610
Natural variant5541P → L.
Corresponds to variant rs12714214 [ dbSNP | Ensembl ].
VAR_020135
Natural variant6181A → V. Ref.3 Ref.5 Ref.53
Corresponds to variant rs679899 [ dbSNP | Ensembl ].
VAR_019828
Natural variant7301V → I. Ref.53
Corresponds to variant rs12691202 [ dbSNP | Ensembl ].
VAR_020136
Natural variant7331V → I.
Corresponds to variant rs1800476 [ dbSNP | Ensembl ].
VAR_016185
Natural variant7411T → N.
Corresponds to variant rs12714192 [ dbSNP | Ensembl ].
VAR_020137
Natural variant8771P → L.
Corresponds to variant rs12714097 [ dbSNP | Ensembl ].
VAR_029342
Natural variant9551P → S.
Corresponds to variant rs13306206 [ dbSNP | Ensembl ].
VAR_056738
Natural variant10861G → S.
Corresponds to variant rs12720801 [ dbSNP | Ensembl ].
VAR_029343
Natural variant11131D → H.
Corresponds to variant rs12713844 [ dbSNP | Ensembl ].
VAR_029344
Natural variant11281R → H. Ref.49
Corresponds to variant rs12713843 [ dbSNP | Ensembl ].
VAR_022611
Natural variant12181Q → E Polymorphism confirmed at protein level. Ref.1 Ref.52
Corresponds to variant rs1041956 [ dbSNP | Ensembl ].
VAR_019829
Natural variant13881R → H.
Corresponds to variant rs13306187 [ dbSNP | Ensembl ].
VAR_029345
Natural variant14221Y → C. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.15
Corresponds to variant rs568413 [ dbSNP | Ensembl ].
VAR_061558
Natural variant14371F → L. Ref.45
Corresponds to variant rs1801697 [ dbSNP | Ensembl ].
VAR_005016
Natural variant16131S → T. Ref.53
VAR_067278
Natural variant16701E → D Polymorphism confirmed at protein level. Ref.8 Ref.52
VAR_068911
Natural variant19141N → S. Ref.45 Ref.47
Corresponds to variant rs1801699 [ dbSNP | Ensembl ].
VAR_005017
Natural variant19231H → R. Ref.47 Ref.53
Corresponds to variant rs533617 [ dbSNP | Ensembl ].
VAR_005018
Natural variant20371I → N Polymorphism confirmed at protein level. Ref.4 Ref.52
VAR_068912
Natural variant20921L → V. Ref.1
Corresponds to variant rs1041960 [ dbSNP | Ensembl ].
VAR_019830
Natural variant22991D → H.
Corresponds to variant rs12713681 [ dbSNP | Ensembl ].
VAR_029346
Natural variant23131I → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.15 Ref.16
Corresponds to variant rs584542 [ dbSNP | Ensembl ].
VAR_059582
Natural variant23651A → T. Ref.1
Corresponds to variant rs1041971 [ dbSNP | Ensembl ].
VAR_019831
Natural variant24561A → D.
Corresponds to variant rs12713675 [ dbSNP | Ensembl ].
VAR_020138
Natural variant25641F → C in a colorectal cancer sample; somatic mutation; polymorphism confirmed at protein level. Ref.50 Ref.52
VAR_035795
Natural variant25661E → K Polymorphism confirmed at protein level. Ref.45 Ref.52 Ref.53
Corresponds to variant rs1801696 [ dbSNP | Ensembl ].
VAR_005019
Natural variant26801L → Q. Ref.1
Corresponds to variant rs1042013 [ dbSNP | Ensembl ].
VAR_019832
Natural variant27391P → L. Ref.43 Ref.47 Ref.53
Corresponds to variant rs676210 [ dbSNP | Ensembl ].
VAR_005020
Natural variant27851N → H.
Corresponds to variant rs2163204 [ dbSNP | Ensembl ].
VAR_022038
Natural variant31211A → T. Ref.45
Corresponds to variant rs1801694 [ dbSNP | Ensembl ].
VAR_005021
Natural variant31821H → N.
Corresponds to variant rs12720848 [ dbSNP | Ensembl ].
VAR_029347
Natural variant32791S → G.
Corresponds to variant rs12720854 [ dbSNP | Ensembl ].
VAR_029348
Natural variant32941S → P.
Corresponds to variant rs12720855 [ dbSNP | Ensembl ].
VAR_020139
Natural variant33191D → H. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.15 Ref.23 Ref.47
VAR_005022
Natural variant34271T → K. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.15 Ref.23 Ref.47
VAR_005023
Natural variant34321Q → E. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.15 Ref.23 Ref.47
Corresponds to variant rs1042023 [ dbSNP | Ensembl ].
VAR_005024
Natural variant35271R → Q in FDB. Ref.42 Ref.46 Ref.51
Corresponds to variant rs5742904 [ dbSNP | Ensembl ].
VAR_005025
Natural variant35581R → C in FDB. Ref.44 Ref.46
Corresponds to variant rs12713559 [ dbSNP | Ensembl ].
VAR_005026
Natural variant36381R → Q. Ref.53
Corresponds to variant rs1801701 [ dbSNP | Ensembl ].
VAR_016186
Natural variant37321I → T. Ref.1 Ref.5 Ref.15 Ref.23
Corresponds to variant rs1042025 [ dbSNP | Ensembl ].
VAR_019833
Natural variant38011S → T.
Corresponds to variant rs12713540 [ dbSNP | Ensembl ].
VAR_029349
Natural variant38351I → L. Ref.53
VAR_067279
Natural variant39211V → I. Ref.47
Corresponds to variant rs72654409 [ dbSNP | Ensembl ].
VAR_005027
Natural variant39451T → A. Ref.45
Corresponds to variant rs1801698 [ dbSNP | Ensembl ].
VAR_005028
Natural variant39491F → L. Ref.1 Ref.4 Ref.5 Ref.23 Ref.25
Corresponds to variant rs1042027 [ dbSNP | Ensembl ].
VAR_019834
Natural variant39641Y → F. Ref.1 Ref.5 Ref.23 Ref.25
Corresponds to variant rs1126468 [ dbSNP | Ensembl ].
VAR_019835
Natural variant41281V → M. Ref.45
Corresponds to variant rs1801703 [ dbSNP | Ensembl ].
VAR_005029
Natural variant41811E → K. Ref.1 Ref.4 Ref.5 Ref.23 Ref.25 Ref.53
Corresponds to variant rs1042031 [ dbSNP | Ensembl ].
VAR_016187
Natural variant42701R → T. Ref.53
Corresponds to variant rs1801702 [ dbSNP | Ensembl ].
VAR_016188
Natural variant43141I → V. Ref.53
Corresponds to variant rs72654423 [ dbSNP | Ensembl ].
VAR_067280
Natural variant43381S → N. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.15 Ref.23 Ref.24 Ref.41 Ref.53
Corresponds to variant rs1042034 [ dbSNP | Ensembl ].
VAR_005030
Natural variant43941V → A.
Corresponds to variant rs12720843 [ dbSNP | Ensembl ].
VAR_029350
Natural variant44811A → T. Ref.45 Ref.53
Corresponds to variant rs1801695 [ dbSNP | Ensembl ].
VAR_005031
Natural variant44821I → V. Ref.53
VAR_067281
Natural variant44841T → M.
Corresponds to variant rs12713450 [ dbSNP | Ensembl ].
VAR_020140

Experimental info

Mutagenesis4831D → N: Impairs protein secretion. Ref.48
Mutagenesis4831D → Q: Does not affect protein secretion. Ref.48
Mutagenesis4901R → A: Impairs protein secretion. Ref.48
Mutagenesis4901R → K: Does not affect protein secretion. Ref.48
Sequence conflict11 – 133Missing in AAB60718. Ref.5
Sequence conflict11 – 133Missing in CAA28420. Ref.5
Sequence conflict3291L → V in AAA35549. Ref.3
Sequence conflict6451L → I in AAA35549. Ref.3
Sequence conflict7041L → P in AAB04636. Ref.4
Sequence conflict792 – 80918LQLLG…TLQGI → SSSWKAASHGCPHSAGD in AAA51759. Ref.12
Sequence conflict7931Q → R in AAB04636. Ref.4
Sequence conflict8931D → K AA sequence Ref.13
Sequence conflict9191A → P in AAA35549. Ref.3
Sequence conflict11091H → D in CAA28420. Ref.5
Sequence conflict11801T → R in AAA51752. Ref.8
Sequence conflict12711F → S in AAB04636. Ref.4
Sequence conflict14181F → S in CAA28420. Ref.5
Sequence conflict14451N → I in AAA51752. Ref.8
Sequence conflict15351G → E in AAA51752. Ref.8
Sequence conflict18671R → G in AAB04636. Ref.4
Sequence conflict20981N → K in CAA28420. Ref.5
Sequence conflict22181I → T in AAB04636. Ref.4
Sequence conflict22211N → I in CAA28420. Ref.5
Sequence conflict2324 – 23263LIG → PYW in AAA51741. Ref.16
Sequence conflict23531Q → H in AAA51741. Ref.16
Sequence conflict25401G → S in CAA28420. Ref.5
Sequence conflict2718 – 273720Missing in AAA51758. Ref.15
Sequence conflict29331C → S in AAB04636. Ref.4
Sequence conflict31141H → L AA sequence Ref.13
Sequence conflict31311T → R AA sequence Ref.13
Sequence conflict31341E → P AA sequence Ref.13
Sequence conflict31371L → R AA sequence Ref.13
Sequence conflict32391H → Q in CAA28420. Ref.5
Sequence conflict32861L → I in AAB04636. Ref.4
Sequence conflict32911R → L in AAA51758. Ref.15
Sequence conflict33371I → N in AAA51758. Ref.15
Sequence conflict34311A → P in AAB04636. Ref.4
Sequence conflict37281D → N in AAA51742. Ref.24
Sequence conflict37821N → T in AAB04636. Ref.4
Sequence conflict38241Q → R in CAA28420. Ref.5
Sequence conflict38241Q → R in AAA51750. Ref.23
Sequence conflict38761V → A in AAA35549. Ref.3
Sequence conflict38761V → A in AAA51742. Ref.24
Sequence conflict39111T → Y AA sequence Ref.10
Sequence conflict39831F → S in AAA51742. Ref.24
Sequence conflict40021A → P in AAA51742. Ref.24
Sequence conflict4110 – 41112NN → DH in AAA35549. Ref.3
Sequence conflict4110 – 41112NN → DH in AAA51742. Ref.24
Sequence conflict41221Q → E in AAA35549. Ref.3
Sequence conflict41221Q → E in AAA51742. Ref.24
Sequence conflict41281V → E in AAA35549. Ref.3
Sequence conflict41281V → E in AAA51742. Ref.24
Sequence conflict41331A → G in AAA35549. Ref.3
Sequence conflict41331A → G in AAA51742. Ref.24
Sequence conflict41881H → K in AAB04636. Ref.4
Sequence conflict4217 – 42182CT → FP in AAA35548. Ref.26
Sequence conflict42211I → M in AAB04636. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P04114 [UniParc].

Last modified July 13, 2010. Version 2.
Checksum: 6800F94BF6ADF698

FASTA4,563515,605
        10         20         30         40         50         60 
MDPPRPALLA LLALPALLLL LLAGARAEEE MLENVSLVCP KDATRFKHLR KYTYNYEAES 

        70         80         90        100        110        120 
SSGVPGTADS RSATRINCKV ELEVPQLCSF ILKTSQCTLK EVYGFNPEGK ALLKKTKNSE 

       130        140        150        160        170        180 
EFAAAMSRYE LKLAIPEGKQ VFLYPEKDEP TYILNIKRGI ISALLVPPET EEAKQVLFLD 

       190        200        210        220        230        240 
TVYGNCSTHF TVKTRKGNVA TEISTERDLG QCDRFKPIRT GISPLALIKG MTRPLSTLIS 

       250        260        270        280        290        300 
SSQSCQYTLD AKRKHVAEAI CKEQHLFLPF SYKNKYGMVA QVTQTLKLED TPKINSRFFG 

       310        320        330        340        350        360 
EGTKKMGLAF ESTKSTSPPK QAEAVLKTLQ ELKKLTISEQ NIQRANLFNK LVTELRGLSD 

       370        380        390        400        410        420 
EAVTSLLPQL IEVSSPITLQ ALVQCGQPQC STHILQWLKR VHANPLLIDV VTYLVALIPE 

       430        440        450        460        470        480 
PSAQQLREIF NMARDQRSRA TLYALSHAVN NYHKTNPTGT QELLDIANYL MEQIQDDCTG 

       490        500        510        520        530        540 
DEDYTYLILR VIGNMGQTME QLTPELKSSI LKCVQSTKPS LMIQKAAIQA LRKMEPKDKD 

       550        560        570        580        590        600 
QEVLLQTFLD DASPGDKRLA AYLMLMRSPS QADINKIVQI LPWEQNEQVK NFVASHIANI 

       610        620        630        640        650        660 
LNSEELDIQD LKKLVKEALK ESQLPTVMDF RKFSRNYQLY KSVSLPSLDP ASAKIEGNLI 

       670        680        690        700        710        720 
FDPNNYLPKE SMLKTTLTAF GFASADLIEI GLEGKGFEPT LEALFGKQGF FPDSVNKALY 

       730        740        750        760        770        780 
WVNGQVPDGV SKVLVDHFGY TKDDKHEQDM VNGIMLSVEK LIKDLKSKEV PEARAYLRIL 

       790        800        810        820        830        840 
GEELGFASLH DLQLLGKLLL MGARTLQGIP QMIGEVIRKG SKNDFFLHYI FMENAFELPT 

       850        860        870        880        890        900 
GAGLQLQISS SGVIAPGAKA GVKLEVANMQ AELVAKPSVS VEFVTNMGII IPDFARSGVQ 

       910        920        930        940        950        960 
MNTNFFHESG LEAHVALKAG KLKFIIPSPK RPVKLLSGGN TLHLVSTTKT EVIPPLIENR 

       970        980        990       1000       1010       1020 
QSWSVCKQVF PGLNYCTSGA YSNASSTDSA SYYPLTGDTR LELELRPTGE IEQYSVSATY 

      1030       1040       1050       1060       1070       1080 
ELQREDRALV DTLKFVTQAE GAKQTEATMT FKYNRQSMTL SSEVQIPDFD VDLGTILRVN 

      1090       1100       1110       1120       1130       1140 
DESTEGKTSY RLTLDIQNKK ITEVALMGHL SCDTKEERKI KGVISIPRLQ AEARSEILAH 

      1150       1160       1170       1180       1190       1200 
WSPAKLLLQM DSSATAYGST VSKRVAWHYD EEKIEFEWNT GTNVDTKKMT SNFPVDLSDY 

      1210       1220       1230       1240       1250       1260 
PKSLHMYANR LLDHRVPQTD MTFRHVGSKL IVAMSSWLQK ASGSLPYTQT LQDHLNSLKE 

      1270       1280       1290       1300       1310       1320 
FNLQNMGLPD FHIPENLFLK SDGRVKYTLN KNSLKIEIPL PFGGKSSRDL KMLETVRTPA 

      1330       1340       1350       1360       1370       1380 
LHFKSVGFHL PSREFQVPTF TIPKLYQLQV PLLGVLDLST NVYSNLYNWS ASYSGGNTST 

      1390       1400       1410       1420       1430       1440 
DHFSLRARYH MKADSVVDLL SYNVQGSGET TYDHKNTFTL SYDGSLRHKF LDSNIKFSHV 

      1450       1460       1470       1480       1490       1500 
EKLGNNPVSK GLLIFDASSS WGPQMSASVH LDSKKKQHLF VKEVKIDGQF RVSSFYAKGT 

      1510       1520       1530       1540       1550       1560 
YGLSCQRDPN TGRLNGESNL RFNSSYLQGT NQITGRYEDG TLSLTSTSDL QSGIIKNTAS 

      1570       1580       1590       1600       1610       1620 
LKYENYELTL KSDTNGKYKN FATSNKMDMT FSKQNALLRS EYQADYESLR FFSLLSGSLN 

      1630       1640       1650       1660       1670       1680 
SHGLELNADI LGTDKINSGA HKATLRIGQD GISTSATTNL KCSLLVLENE LNAELGLSGA 

      1690       1700       1710       1720       1730       1740 
SMKLTTNGRF REHNAKFSLD GKAALTELSL GSAYQAMILG VDSKNIFNFK VSQEGLKLSN 

      1750       1760       1770       1780       1790       1800 
DMMGSYAEMK FDHTNSLNIA GLSLDFSSKL DNIYSSDKFY KQTVNLQLQP YSLVTTLNSD 

      1810       1820       1830       1840       1850       1860 
LKYNALDLTN NGKLRLEPLK LHVAGNLKGA YQNNEIKHIY AISSAALSAS YKADTVAKVQ 

      1870       1880       1890       1900       1910       1920 
GVEFSHRLNT DIAGLASAID MSTNYNSDSL HFSNVFRSVM APFTMTIDAH TNGNGKLALW 

      1930       1940       1950       1960       1970       1980 
GEHTGQLYSK FLLKAEPLAF TFSHDYKGST SHHLVSRKSI SAALEHKVSA LLTPAEQTGT 

      1990       2000       2010       2020       2030       2040 
WKLKTQFNNN EYSQDLDAYN TKDKIGVELT GRTLADLTLL DSPIKVPLLL SEPINIIDAL 

      2050       2060       2070       2080       2090       2100 
EMRDAVEKPQ EFTIVAFVKY DKNQDVHSIN LPFFETLQEY FERNRQTIIV VLENVQRNLK 

      2110       2120       2130       2140       2150       2160 
HINIDQFVRK YRAALGKLPQ QANDYLNSFN WERQVSHAKE KLTALTKKYR ITENDIQIAL 

      2170       2180       2190       2200       2210       2220 
DDAKINFNEK LSQLQTYMIQ FDQYIKDSYD LHDLKIAIAN IIDEIIEKLK SLDEHYHIRV 

      2230       2240       2250       2260       2270       2280 
NLVKTIHDLH LFIENIDFNK SGSSTASWIQ NVDTKYQIRI QIQEKLQQLK RHIQNIDIQH 

      2290       2300       2310       2320       2330       2340 
LAGKLKQHIE AIDVRVLLDQ LGTTISFERI NDILEHVKHF VINLIGDFEV AEKINAFRAK 

      2350       2360       2370       2380       2390       2400 
VHELIERYEV DQQIQVLMDK LVELAHQYKL KETIQKLSNV LQQVKIKDYF EKLVGFIDDA 

      2410       2420       2430       2440       2450       2460 
VKKLNELSFK TFIEDVNKFL DMLIKKLKSF DYHQFVDETN DKIREVTQRL NGEIQALELP 

      2470       2480       2490       2500       2510       2520 
QKAEALKLFL EETKATVAVY LESLQDTKIT LIINWLQEAL SSASLAHMKA KFRETLEDTR 

      2530       2540       2550       2560       2570       2580 
DRMYQMDIQQ ELQRYLSLVG QVYSTLVTYI SDWWTLAAKN LTDFAEQYSI QDWAKRMKAL 

      2590       2600       2610       2620       2630       2640 
VEQGFTVPEI KTILGTMPAF EVSLQALQKA TFQTPDFIVP LTDLRIPSVQ INFKDLKNIK 

      2650       2660       2670       2680       2690       2700 
IPSRFSTPEF TILNTFHIPS FTIDFVEMKV KIIRTIDQML NSELQWPVPD IYLRDLKVED 

      2710       2720       2730       2740       2750       2760 
IPLARITLPD FRLPEIAIPE FIIPTLNLND FQVPDLHIPE FQLPHISHTI EVPTFGKLYS 

      2770       2780       2790       2800       2810       2820 
ILKIQSPLFT LDANADIGNG TTSANEAGIA ASITAKGESK LEVLNFDFQA NAQLSNPKIN 

      2830       2840       2850       2860       2870       2880 
PLALKESVKF SSKYLRTEHG SEMLFFGNAI EGKSNTVASL HTEKNTLELS NGVIVKINNQ 

      2890       2900       2910       2920       2930       2940 
LTLDSNTKYF HKLNIPKLDF SSQADLRNEI KTLLKAGHIA WTSSGKGSWK WACPRFSDEG 

      2950       2960       2970       2980       2990       3000 
THESQISFTI EGPLTSFGLS NKINSKHLRV NQNLVYESGS LNFSKLEIQS QVDSQHVGHS 

      3010       3020       3030       3040       3050       3060 
VLTAKGMALF GEGKAEFTGR HDAHLNGKVI GTLKNSLFFS AQPFEITAST NNEGNLKVRF 

      3070       3080       3090       3100       3110       3120 
PLRLTGKIDF LNNYALFLSP SAQQASWQVS ARFNQYKYNQ NFSAGNNENI MEAHVGINGE 

      3130       3140       3150       3160       3170       3180 
ANLDFLNIPL TIPEMRLPYT IITTPPLKDF SLWEKTGLKE FLKTTKQSFD LSVKAQYKKN 

      3190       3200       3210       3220       3230       3240 
KHRHSITNPL AVLCEFISQS IKSFDRHFEK NRNNALDFVT KSYNETKIKF DKYKAEKSHD 

      3250       3260       3270       3280       3290       3300 
ELPRTFQIPG YTVPVVNVEV SPFTIEMSAF GYVFPKAVSM PSFSILGSDV RVPSYTLILP 

      3310       3320       3330       3340       3350       3360 
SLELPVLHVP RNLKLSLPDF KELCTISHIF IPAMGNITYD FSFKSSVITL NTNAELFNQS 

      3370       3380       3390       3400       3410       3420 
DIVAHLLSSS SSVIDALQYK LEGTTRLTRK RGLKLATALS LSNKFVEGSH NSTVSLTTKN 

      3430       3440       3450       3460       3470       3480 
MEVSVATTTK AQIPILRMNF KQELNGNTKS KPTVSSSMEF KYDFNSSMLY STAKGAVDHK 

      3490       3500       3510       3520       3530       3540 
LSLESLTSYF SIESSTKGDV KGSVLSREYS GTIASEANTY LNSKSTRSSV KLQGTSKIDD 

      3550       3560       3570       3580       3590       3600 
IWNLEVKENF AGEATLQRIY SLWEHSTKNH LQLEGLFFTN GEHTSKATLE LSPWQMSALV 

      3610       3620       3630       3640       3650       3660 
QVHASQPSSF HDFPDLGQEV ALNANTKNQK IRWKNEVRIH SGSFQSQVEL SNDQEKAHLD 

      3670       3680       3690       3700       3710       3720 
IAGSLEGHLR FLKNIILPVY DKSLWDFLKL DVTTSIGRRQ HLRVSTAFVY TKNPNGYSFS 

      3730       3740       3750       3760       3770       3780 
IPVKVLADKF IIPGLKLNDL NSVLVMPTFH VPFTDLQVPS CKLDFREIQI YKKLRTSSFA 

      3790       3800       3810       3820       3830       3840 
LNLPTLPEVK FPEVDVLTKY SQPEDSLIPF FEITVPESQL TVSQFTLPKS VSDGIAALDL 

      3850       3860       3870       3880       3890       3900 
NAVANKIADF ELPTIIVPEQ TIEIPSIKFS VPAGIVIPSF QALTARFEVD SPVYNATWSA 

      3910       3920       3930       3940       3950       3960 
SLKNKADYVE TVLDSTCSST VQFLEYELNV LGTHKIEDGT LASKTKGTFA HRDFSAEYEE 

      3970       3980       3990       4000       4010       4020 
DGKYEGLQEW EGKAHLNIKS PAFTDLHLRY QKDKKGISTS AASPAVGTVG MDMDEDDDFS 

      4030       4040       4050       4060       4070       4080 
KWNFYYSPQS SPDKKLTIFK TELRVRESDE ETQIKVNWEE EAASGLLTSL KDNVPKATGV 

      4090       4100       4110       4120       4130       4140 
LYDYVNKYHW EHTGLTLREV SSKLRRNLQN NAEWVYQGAI RQIDDIDVRF QKAASGTTGT 

      4150       4160       4170       4180       4190       4200 
YQEWKDKAQN LYQELLTQEG QASFQGLKDN VFDGLVRVTQ EFHMKVKHLI DSLIDFLNFP 

      4210       4220       4230       4240       4250       4260 
RFQFPGKPGI YTREELCTMF IREVGTVLSQ VYSKVHNGSE ILFSYFQDLV ITLPFELRKH 

      4270       4280       4290       4300       4310       4320 
KLIDVISMYR ELLKDLSKEA QEVFKAIQSL KTTEVLRNLQ DLLQFIFQLI EDNIKQLKEM 

      4330       4340       4350       4360       4370       4380 
KFTYLINYIQ DEINTIFSDY IPYVFKLLKE NLCLNLHKFN EFIQNELQEA SQELQQIHQY 

      4390       4400       4410       4420       4430       4440 
IMALREEYFD PSIVGWTVKY YELEEKIVSL IKNLLVALKD FHSEYIVSAS NFTSQLSSQV 

      4450       4460       4470       4480       4490       4500 
EQFLHRNIQE YLSILTDPDG KGKEKIAELS ATAQEIIKSQ AIATKKIISD YHQQFRYKLQ 

      4510       4520       4530       4540       4550       4560 
DFSDQLSDYY EKFIAESKRL IDLSIQNYHT FLIYITELLK KLQSTTVMNP YMKLAPGELT 


IIL 

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References

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[1]"Complete cDNA and derived protein sequence of human apolipoprotein B-100."
Knott T.C., Wallis S.C., Powell L.M., Pease R.J., Lusis A.J., Blackhart B., McCarthy B.J., Mahley R.W., Levy-Wilson B., Scott J.
Nucleic Acids Res. 14:7501-7503(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-273; GLU-1218; CYS-1422; RP VAL-2092; VAL-2313; THR-2365; GLN-2680; HIS-3319; LYS-3427; GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
[2]"DNA sequence of the human apolipoprotein B gene."
Ludwig E.H., Blackhart B.D., Pierotti V.R., Caiati L., Fortier C., Knott T., Scott J., Mahley R.W., Levy-Wilson B., McCarthy B.J.
DNA 6:363-372(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
[3]"The complete cDNA and amino acid sequence of human apolipoprotein B-100."
Chen S.-H., Yang C.-Y., Chen P.-F., Setzer D., Tanimura M., Li W.-H., Gotto A.M. Jr., Chan L.
J. Biol. Chem. 261:12918-12921(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-98; VAL-618; CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
[4]"Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence."
Law S.W., Grant S.M., Higuchi K., Hospattankar A.V., Lackner K.J., Lee N., Brewer H.B. Jr.
Proc. Natl. Acad. Sci. U.S.A. 83:8142-8146(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CYS-1422; ASN-2037; VAL-2313; HIS-3319; LYS-3427; GLU-3432; LEU-3949; LYS-4181 AND ASN-4338.
[5]"The complete sequence and structural analysis of human apolipoprotein B-100: relationship between apoB-100 and apoB-48 forms."
Cladaras C., Hadzopoulou-Cladaras M., Nolte R.T., Atkinson D., Zannis V.I.
EMBO J. 5:3495-3507(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40, VARIANTS VAL-618; CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
[6]SeattleSNPs variation discovery resource
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-1422; VAL-2313 AND ASN-4338.
[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. expand/collapse author list , 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]"Analysis of cDNA clones encoding the entire B-26 region of human apolipoprotein B."
Protter A.A., Hardman D.A., Sato K.Y., Schilling J.W., Yamanaka M., Hort Y.J., Hjerrild K.A., Chen G.C., Kane J.P.
Proc. Natl. Acad. Sci. U.S.A. 83:5678-5682(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1670, VARIANTS ILE-98; CYS-1422 AND ASP-1670.
[9]"Isolation of a cDNA clone encoding the amino-terminal region of human apolipoprotein B."
Protter A.A., Hardman D.A., Schilling J.W., Miller J., Appleby V., Chen G.C., Kirsher S.W., McEnroe G., Kane J.P.
Proc. Natl. Acad. Sci. U.S.A. 83:1467-1471(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-291.
[10]"Isolation and characterization of sulfhydryl and disulfide peptides of human apolipoprotein B-100."
Yang C.Y., Kim T.W., Weng S.A., Lee B.R., Yang M.L., Gotto A.M. Jr.
Proc. Natl. Acad. Sci. U.S.A. 87:5523-5527(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, VARIANT ILE-98.
[11]"Human apolipoprotein B-100: cloning, analysis of liver mRNA, and assignment of the gene to chromosome 2."
Law S.W., Lackner K.J., Hospattankar A.V., Anchors J.M., Sakaguchi A.Y., Naylor S.L., Brewer H.B. Jr.
Proc. Natl. Acad. Sci. U.S.A. 82:8340-8344(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 485-1044.
Tissue: Liver.
[12]"A partial cDNA clone for human apolipoprotein B."
Deeb S.S., Motulsky A.G., Albers J.J.
Proc. Natl. Acad. Sci. U.S.A. 82:4983-4986(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 709-906.
[13]"Human apolipoprotein B: partial amino acid sequence."
LeBoeuf R.C., Miller C., Shively J.E., Schumaker V.N., Balla M.A., Lusis A.J.
FEBS Lett. 170:105-108(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 873-896 AND 3113-3137.
[14]"Hypobetalipoproteinemia due to an apolipoprotein B gene exon 21 deletion derived by Alu-Alu recombination."
Huang L.S., Ripps M.E., Korman S.H., Deckelbaum R.J., Breslow J.L.
J. Biol. Chem. 264:11394-11400(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1042-1232.
[15]"Analysis of the human apolipoprotein B gene; complete structure of the B-74 region."
Carlsson P., Darnfors C., Olofsson S.O., Bjursell G.
Gene 49:29-51(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1282-4503, VARIANTS CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432; THR-3732 AND ASN-4338.
[16]"Structural comparison of human apolipoproteins B-48 and B-100."
Hardman D.A., Protter A.A., Chen G.C., Schilling J.W., Sato K.Y., Lau K., Yamanaka M., Mikita T., Miller J., Crisp T., McEnroe G., Scarborough R.M., Kane J.P.
Biochemistry 26:5478-5486(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1671-2398, VARIANT VAL-2313.
[17]"Molecular cloning of human apolipoprotein B cDNA."
Carlsson P., Olofsson S.O., Bondjers G., Darnfors C., Wiklund O., Bjursell G.
Nucleic Acids Res. 13:8813-8826(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1937-2018 AND 3811-4334.
[18]"A novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine."
Powell L.M., Wallis S.C., Pease R.J., Edwards Y.H., Knott T.J., Scott J.
Cell 50:831-840(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2115-2179.
Tissue: Small intestine.
[19]"Human apolipoprotein B (apoB) mRNA: identification of two distinct apoB mRNAs, an mRNA with the apoB-100 sequence and an apoB mRNA containing a premature in-frame translational stop codon, in both liver and intestine."
Higuchi K., Hospattankar A.V., Law S.W., Meglin N., Cortright J., Brewer H.B. Jr.
Proc. Natl. Acad. Sci. U.S.A. 85:1772-1776(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2127-2179.
[20]"Carboxyl terminal analysis of human B-48 protein confirms the novel mechanism proposed for chain termination."
Hardman D.A., Protter A.A., Schilling J.W., Kane J.P.
Biochem. Biophys. Res. Commun. 149:1214-1219(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2129-2235.
[21]"Identification of a novel in-frame translational stop codon in human intestine apoB mRNA."
Hospattankar A.V., Higuchi K., Law S.W., Meglin N., Brewer H.B. Jr.
Biochem. Biophys. Res. Commun. 148:279-285(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2169-2179.
[22]"Human apolipoprotein B: identification of cDNA clones and characterization of mRNA."
Mehrabian M., Schumaker V.N., Fareed G.C., West R., Johnson D.F., Kirchgessner T.G., Lin H.-C., Wang X., Ma Y., Mendiaz E., Lusis A.J.
Nucleic Acids Res. 13:6937-6953(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3056-3159.
[23]"Human apolipoprotein B: structure of carboxyl-terminal domains, sites of gene expression, and chromosomal localization."
Knott T.J., Rall S.C. Jr., Innerarity T.L., Jacobson S.F., Urdea M.S., Levy-Wilson B., Powell L.M., Pease R.J., Eddy R., Nakai H., Byers M., Priestley L.M., Robertson E., Rall L.B., Betsholtz C., Shows T.B., Mahley R.W., Scott J.
Science 230:37-43(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3109-4563, VARIANTS HIS-3319; LYS-3427; GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
[24]"Molecular cloning and expression of partial cDNAs and deduced amino acid sequence of a carboxyl-terminal fragment of human apolipoprotein B-100."
Wei C.F., Chen S.H., Yang C.Y., Marcel Y.L., Milne R.W., Li W.H., Sparrow J.T., Gotto A.M. Jr., Chan L.
Proc. Natl. Acad. Sci. U.S.A. 82:7265-7269(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3728-4563, VARIANT ASN-4338.
[25]"Molecular cloning of human LDL apolipoprotein B cDNA. Evidence for more than one gene per haploid genome."
Shoulders C.C., Myant N.B., Sidoli A., Rodriguez J.C., Cortese C., Baralle F.E., Cortese R.
Atherosclerosis 58:277-289(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3846-4298, VARIANTS LEU-3949; PHE-3964 AND LYS-4181.
Tissue: Liver.
[26]"Isolation, expression and characterization of a human apolipoprotein B 100-specific cDNA clone."
Pfitzner R., Wagener R., Stoffel W.
Biol. Chem. Hoppe-Seyler 367:1077-1083(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4217-4563.
[27]"Apolipoprotein B-48 is the product of a messenger RNA with an organ-specific in-frame stop codon."
Chen S.-H., Habib G., Yang C.-H., Gu Z.-W., Lee B.R., Weng S.-H., Silberman S.R., Cai S.-J., Deslypere J.P., Rosseneu M., Gotto A.M. Jr., Li W.-H., Chan L.
Science 238:363-366(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION OF APO-B48.
[28]"Complete protein sequence and identification of structural domains of human apolipoprotein B."
Knott T.C., Pease R.J., Powell L.M., Wallis S.C., Rall S.C. Jr., Innerarity T.L., Blackhart B., Taylor W.R., Marcel Y., Milne R., Johnson D., Fuller M., Lusis A.J., McCarthy B.J., Mahley R.W., Levy-Wilson B., Scott J.
Nature 323:734-738(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS.
[29]"Sequence, structure, receptor-binding domains and internal repeats of human apolipoprotein B-100."
Yang C.-Y., Chen S.-H., Gianturco S.H., Bradley W.A., Sparrow J.T., Tanimura M., Li W.-H., Sparrow D.A., Deloof H., Rosseneu M., Lee F.-S., Gu Z.-W., Gotto A.M. Jr., Chan L.
Nature 323:738-742(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS.
[30]"Apolipoprotein B is a calcium binding protein."
Dashti N., Lee D.M., Mok T.
Biochem. Biophys. Res. Commun. 137:493-499(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM-BINDING.
[31]"Palmitoylation of apolipoprotein B is required for proper intracellular sorting and transport of cholesteroyl esters and triglycerides."
Zhao Y., McCabe J.B., Vance J., Berthiaume L.G.
Mol. Biol. Cell 11:721-734(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-1112.
[32]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3358.
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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-2564.
[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.
+Additional computationally mapped references.

Web resources

GeneReviews
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Apolipoprotein B entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04506 mRNA. Translation: CAA28191.1.
M19828 expand/collapse EMBL AC list , 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.
PIRLPHUB. A27850.
RefSeqNP_000375.2. NM_000384.2.
UniGeneHs.120759.

3D structure databases

ProteinModelPortalP04114.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106835. 39 interactions.
DIPDIP-44767N.
IntActP04114. 13 interactions.
MINTMINT-1506918.

Chemistry

BindingDBP04114.
ChEMBLCHEMBL4549.
DrugBankDB01076. Atorvastatin.

PTM databases

PhosphoSiteP04114.
UniCarbKBP04114.

Polymorphism databases

DMDM300669605.

Proteomic databases

PaxDbP04114.
PeptideAtlasP04114.
PRIDEP04114.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233242; ENSP00000233242; ENSG00000084674.
GeneID338.
KEGGhsa:338.

Organism-specific databases

CTD338.
GeneCardsGC02M021135.
H-InvDBHIX0024005.
HGNCHGNC:603. APOB.
HPACAB016070.
HPA049793.
MIM107730. gene+phenotype.
144010. phenotype.
615558. phenotype.
neXtProtNX_P04114.
Orphanet406. Familial hypercholesterolemia.
426. Familial hypobetalipoproteinemia.
PharmGKBPA50.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290405.
HOVERGENHBG050546.
InParanoidP04114.
KOK14462.
OMAHIPEFQL.
OrthoDBEOG7VB2DG.
PhylomeDBP04114.
TreeFamTF331316.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP04114.
BgeeP04114.
GenevestigatorP04114.

Family and domain databases

Gene3D1.25.10.20. 1 hit.
2.20.50.20. 2 hits.
2.20.80.10. 1 hit.
2.30.230.10. 1 hit.
InterProIPR022176. 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]
PfamPF12491. ApoB100_C. 1 hit.
PF06448. DUF1081. 1 hit.
PF09172. DUF1943. 1 hit.
PF01347. Vitellogenin_N. 1 hit.
[Graphical view]
SMARTSM00638. LPD_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
SSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 2 hits.
PROSITEPS51211. VITELLOGENIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPOB. human.
GeneWikiApolipoprotein_B.
GenomeRNAi338.
NextBio1399.
PROP04114.
SOURCESearch...

Entry information

Entry nameAPOB_HUMAN
AccessionPrimary (citable) accession number: P04114
Secondary accession number(s): O00502 expand/collapse secondary AC list , P78479, P78480, P78481, Q13779, Q13785, Q13786, Q13787, Q13788, Q4ZG63, Q53QC8, Q7Z600, Q9UMN0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: July 13, 2010
Last modified: April 16, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM