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P04114

- APOB_HUMAN

UniProt

P04114 - APOB_HUMAN

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Protein
Apolipoprotein B-100
Gene
APOB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. cholesterol transporter activity Source: BHF-UCL
  2. heparin binding Source: BHF-UCL
  3. lipase binding Source: BHF-UCL
  4. low-density lipoprotein particle receptor binding Source: BHF-UCL
  5. phospholipid binding Source: BHF-UCL
  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. sperm motility Source: Ensembl
  33. spermatogenesis Source: Ensembl
  34. triglyceride catabolic process Source: Ensembl
  35. triglyceride mobilization Source: Ensembl
  36. very-low-density lipoprotein particle assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

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

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

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

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:603. APOB.

Subcellular locationi

Cytoplasm. Secreted 1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: HPA
  2. actin cytoskeleton Source: HPA
  3. chylomicron Source: BHF-UCL
  4. chylomicron remnant Source: BHF-UCL
  5. clathrin-coated endocytic vesicle membrane Source: Reactome
  6. cytoplasm Source: UniProtKB
  7. cytosol Source: Reactome
  8. early endosome Source: Reactome
  9. endocytic vesicle lumen Source: Reactome
  10. endoplasmic reticulum lumen Source: Reactome
  11. endoplasmic reticulum membrane Source: Reactome
  12. endosome lumen Source: Reactome
  13. endosome membrane Source: Reactome
  14. extracellular region Source: Reactome
  15. extracellular space Source: BHF-UCL
  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
Complete GO annotation...

Keywords - Cellular componenti

Chylomicron, Cytoplasm, LDL, Secreted, VLDL

Pathology & Biotechi

Involvement in diseasei

Hypobetalipoproteinemia, familial, 1 (FHBL1) [MIM:615558]: A disorder of lipid metabolism characterized by less than 5th percentile age- and sex-specific levels of low density lipoproteins, and dietary fat malabsorption. Clinical presentation may vary from no symptoms to severe gastrointestinal and neurological dysfunction similar to abetalipoproteinemia.
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 (1 Publication).2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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 – 2727
Add
BLAST
Chaini28 – 45634536Apolipoprotein B-100
PRO_0000020750Add
BLAST
Chaini28 – 21792152Apolipoprotein B-48
PRO_0000020751Add
BLAST

Amino acid modifications

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

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. 14 interactions.
MINTiMINT-1506918.

Structurei

3D structure databases

ProteinModelPortaliP04114.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 672627Vitellogenin
Add
BLAST

Region

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

Sequence similaritiesi

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 133Missing in AAB60718. 1 Publication
Sequence conflicti11 – 133Missing in CAA28420. 1 Publication
Sequence conflicti329 – 3291L → V in AAA35549. 1 Publication
Sequence conflicti645 – 6451L → I in AAA35549. 1 Publication
Sequence conflicti704 – 7041L → P in AAB04636. 1 Publication
Sequence conflicti792 – 80918LQLLG…TLQGI → SSSWKAASHGCPHSAGD in AAA51759. 1 Publication
Add
BLAST
Sequence conflicti793 – 7931Q → R in AAB04636. 1 Publication
Sequence conflicti893 – 8931D → K AA sequence 1 Publication
Sequence conflicti919 – 9191A → P in AAA35549. 1 Publication
Sequence conflicti1109 – 11091H → D in CAA28420. 1 Publication
Sequence conflicti1180 – 11801T → R in AAA51752. 1 Publication
Sequence conflicti1271 – 12711F → S in AAB04636. 1 Publication
Sequence conflicti1418 – 14181F → S in CAA28420. 1 Publication
Sequence conflicti1445 – 14451N → I in AAA51752. 1 Publication
Sequence conflicti1535 – 15351G → E in AAA51752. 1 Publication
Sequence conflicti1867 – 18671R → G in AAB04636. 1 Publication
Sequence conflicti2098 – 20981N → K in CAA28420. 1 Publication
Sequence conflicti2218 – 22181I → T in AAB04636. 1 Publication
Sequence conflicti2221 – 22211N → I in CAA28420. 1 Publication
Sequence conflicti2324 – 23263LIG → PYW in AAA51741. 1 Publication
Sequence conflicti2353 – 23531Q → H in AAA51741. 1 Publication
Sequence conflicti2540 – 25401G → S in CAA28420. 1 Publication
Sequence conflicti2718 – 273720Missing in AAA51758. 1 Publication
Add
BLAST
Sequence conflicti2933 – 29331C → S in AAB04636. 1 Publication
Sequence conflicti3114 – 31141H → L AA sequence 1 Publication
Sequence conflicti3131 – 31311T → R AA sequence 1 Publication
Sequence conflicti3134 – 31341E → P AA sequence 1 Publication
Sequence conflicti3137 – 31371L → R AA sequence 1 Publication
Sequence conflicti3239 – 32391H → Q in CAA28420. 1 Publication
Sequence conflicti3286 – 32861L → I in AAB04636. 1 Publication
Sequence conflicti3291 – 32911R → L in AAA51758. 1 Publication
Sequence conflicti3337 – 33371I → N in AAA51758. 1 Publication
Sequence conflicti3431 – 34311A → P in AAB04636. 1 Publication
Sequence conflicti3728 – 37281D → N in AAA51742. 1 Publication
Sequence conflicti3782 – 37821N → T in AAB04636. 1 Publication
Sequence conflicti3824 – 38241Q → R in CAA28420. 1 Publication
Sequence conflicti3824 – 38241Q → R in AAA51750. 1 Publication
Sequence conflicti3876 – 38761V → A in AAA35549. 1 Publication
Sequence conflicti3876 – 38761V → A in AAA51742. 1 Publication
Sequence conflicti3911 – 39111T → Y AA sequence 1 Publication
Sequence conflicti3983 – 39831F → S in AAA51742. 1 Publication
Sequence conflicti4002 – 40021A → P in AAA51742. 1 Publication
Sequence conflicti4110 – 41112NN → DH in AAA35549. 1 Publication
Sequence conflicti4110 – 41112NN → DH in AAA51742. 1 Publication
Sequence conflicti4122 – 41221Q → E in AAA35549. 1 Publication
Sequence conflicti4122 – 41221Q → E in AAA51742. 1 Publication
Sequence conflicti4128 – 41281V → E in AAA35549. 1 Publication
Sequence conflicti4128 – 41281V → E in AAA51742. 1 Publication
Sequence conflicti4133 – 41331A → G in AAA35549. 1 Publication
Sequence conflicti4133 – 41331A → G in AAA51742. 1 Publication
Sequence conflicti4188 – 41881H → K in AAB04636. 1 Publication
Sequence conflicti4217 – 42182CT → FP in AAA35548. 1 Publication
Sequence conflicti4221 – 42211I → M in AAB04636. 1 Publication

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. 14 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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-273; GLU-1218; CYS-1422; RP VAL-2092; VAL-2313; THR-2365; GLN-2680; HIS-3319; LYS-3427; GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
  3. "The complete cDNA and amino acid sequence of human apolipoprotein B-100."
    Chen S.-H., Yang C.-Y., Chen P.-F., Setzer D., Tanimura M., Li W.-H., Gotto A.M. Jr., Chan L.
    J. Biol. Chem. 261:12918-12921(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-98; VAL-618; CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
  4. "Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence."
    Law S.W., Grant S.M., Higuchi K., Hospattankar A.V., Lackner K.J., Lee N., Brewer H.B. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 83:8142-8146(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CYS-1422; ASN-2037; VAL-2313; HIS-3319; LYS-3427; GLU-3432; LEU-3949; LYS-4181 AND ASN-4338.
  5. "The complete sequence and structural analysis of human apolipoprotein B-100: relationship between apoB-100 and apoB-48 forms."
    Cladaras C., Hadzopoulou-Cladaras M., Nolte R.T., Atkinson D., Zannis V.I.
    EMBO J. 5:3495-3507(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40, VARIANTS VAL-618; CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
  6. SeattleSNPs variation discovery resource
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-1422; VAL-2313 AND ASN-4338.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1670, VARIANTS ILE-98; CYS-1422 AND ASP-1670.
  9. "Isolation of a cDNA clone encoding the amino-terminal region of human apolipoprotein B."
    Protter A.A., Hardman D.A., Schilling J.W., Miller J., Appleby V., Chen G.C., Kirsher S.W., McEnroe G., Kane J.P.
    Proc. Natl. Acad. Sci. U.S.A. 83:1467-1471(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-291.
  10. "Isolation and characterization of sulfhydryl and disulfide peptides of human apolipoprotein B-100."
    Yang C.Y., Kim T.W., Weng S.A., Lee B.R., Yang M.L., Gotto A.M. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 87:5523-5527(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, VARIANT ILE-98.
  11. "Human apolipoprotein B-100: cloning, analysis of liver mRNA, and assignment of the gene to chromosome 2."
    Law S.W., Lackner K.J., Hospattankar A.V., Anchors J.M., Sakaguchi A.Y., Naylor S.L., Brewer H.B. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 82:8340-8344(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 485-1044.
    Tissue: Liver.
  12. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 709-906.
  13. Cited for: PROTEIN SEQUENCE OF 873-896 AND 3113-3137.
  14. "Hypobetalipoproteinemia due to an apolipoprotein B gene exon 21 deletion derived by Alu-Alu recombination."
    Huang L.S., Ripps M.E., Korman S.H., Deckelbaum R.J., Breslow J.L.
    J. Biol. Chem. 264:11394-11400(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1042-1232.
  15. "Analysis of the human apolipoprotein B gene; complete structure of the B-74 region."
    Carlsson P., Darnfors C., Olofsson S.O., Bjursell G.
    Gene 49:29-51(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1282-4503, VARIANTS CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432; THR-3732 AND ASN-4338.
  16. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1671-2398, VARIANT VAL-2313.
  17. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1937-2018 AND 3811-4334.
  18. "A novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine."
    Powell L.M., Wallis S.C., Pease R.J., Edwards Y.H., Knott T.J., Scott J.
    Cell 50:831-840(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2115-2179.
    Tissue: Small intestine.
  19. "Human apolipoprotein B (apoB) mRNA: identification of two distinct apoB mRNAs, an mRNA with the apoB-100 sequence and an apoB mRNA containing a premature in-frame translational stop codon, in both liver and intestine."
    Higuchi K., Hospattankar A.V., Law S.W., Meglin N., Cortright J., Brewer H.B. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 85:1772-1776(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2127-2179.
  20. "Carboxyl terminal analysis of human B-48 protein confirms the novel mechanism proposed for chain termination."
    Hardman D.A., Protter A.A., Schilling J.W., Kane J.P.
    Biochem. Biophys. Res. Commun. 149:1214-1219(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2129-2235.
  21. "Identification of a novel in-frame translational stop codon in human intestine apoB mRNA."
    Hospattankar A.V., Higuchi K., Law S.W., Meglin N., Brewer H.B. Jr.
    Biochem. Biophys. Res. Commun. 148:279-285(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2169-2179.
  22. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3056-3159.
  23. "Human apolipoprotein B: structure of carboxyl-terminal domains, sites of gene expression, and chromosomal localization."
    Knott T.J., Rall S.C. Jr., Innerarity T.L., Jacobson S.F., Urdea M.S., Levy-Wilson B., Powell L.M., Pease R.J., Eddy R., Nakai H., Byers M., Priestley L.M., Robertson E., Rall L.B., Betsholtz C., Shows T.B., Mahley R.W., Scott J.
    Science 230:37-43(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3109-4563, VARIANTS HIS-3319; LYS-3427; GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
  24. "Molecular cloning and expression of partial cDNAs and deduced amino acid sequence of a carboxyl-terminal fragment of human apolipoprotein B-100."
    Wei C.F., Chen S.H., Yang C.Y., Marcel Y.L., Milne R.W., Li W.H., Sparrow J.T., Gotto A.M. Jr., Chan L.
    Proc. Natl. Acad. Sci. U.S.A. 82:7265-7269(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3728-4563, VARIANT ASN-4338.
  25. "Molecular cloning of human LDL apolipoprotein B cDNA. Evidence for more than one gene per haploid genome."
    Shoulders C.C., Myant N.B., Sidoli A., Rodriguez J.C., Cortese C., Baralle F.E., Cortese R.
    Atherosclerosis 58:277-289(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3846-4298, VARIANTS LEU-3949; PHE-3964 AND LYS-4181.
    Tissue: Liver.
  26. "Isolation, expression and characterization of a human apolipoprotein B 100-specific cDNA clone."
    Pfitzner R., Wagener R., Stoffel W.
    Biol. Chem. Hoppe-Seyler 367:1077-1083(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4217-4563.
  27. "Apolipoprotein B-48 is the product of a messenger RNA with an organ-specific in-frame stop codon."
    Chen S.-H., Habib G., Yang C.-H., Gu Z.-W., Lee B.R., Weng S.-H., Silberman S.R., Cai S.-J., Deslypere J.P., Rosseneu M., Gotto A.M. Jr., Li W.-H., Chan L.
    Science 238:363-366(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION OF APO-B48.
  28. Cited for: DOMAINS.
  29. "Sequence, structure, receptor-binding domains and internal repeats of human apolipoprotein B-100."
    Yang C.-Y., Chen S.-H., Gianturco S.H., Bradley W.A., Sparrow J.T., Tanimura M., Li W.-H., Sparrow D.A., Deloof H., Rosseneu M., Lee F.-S., Gu Z.-W., Gotto A.M. Jr., Chan L.
    Nature 323:738-742(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  30. Cited for: CALCIUM-BINDING.
  31. "Palmitoylation of apolipoprotein B is required for proper intracellular sorting and transport of cholesteroyl esters and triglycerides."
    Zhao Y., McCabe J.B., Vance J., Berthiaume L.G.
    Mol. Biol. Cell 11:721-734(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-1112.
  32. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3358.
    Tissue: Plasma.
  33. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1523; ASN-2982; ASN-3465 AND ASN-3895.
    Tissue: Plasma.
  34. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
    Leong W.F., Chow V.T.
    Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  35. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185; ASN-1523; ASN-2239; ASN-2779; ASN-2982; ASN-3101; ASN-3224; ASN-3411; ASN-3465 AND ASN-3895.
    Tissue: Liver.
  36. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2004, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Biological, clinical and population relevance of 95 loci for blood lipids."
    Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C., Stylianou I.M., Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I., Willer C.J., Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M., Barbalic M., Ricketts S.L., Bis J.C., Aulchenko Y.S.
    , Thorleifsson G., Feitosa M.F., Chambers J., Orho-Melander M., Melander O., Johnson T., Li X., Guo X., Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y., Park T., Kim K., Sim X., Twee-Hee Ong R., Croteau-Chonka D.C., Lange L.A., Smith J.D., Song K., Hua Zhao J., Yuan X., Luan J., Lamina C., Ziegler A., Zhang W., Zee R.Y., Wright A.F., Witteman J.C., Wilson J.F., Willemsen G., Wichmann H.E., Whitfield J.B., Waterworth D.M., Wareham N.J., Waeber G., Vollenweider P., Voight B.F., Vitart V., Uitterlinden A.G., Uda M., Tuomilehto J., Thompson J.R., Tanaka T., Surakka I., Stringham H.M., Spector T.D., Soranzo N., Smit J.H., Sinisalo J., Silander K., Sijbrands E.J., Scuteri A., Scott J., Schlessinger D., Sanna S., Salomaa V., Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M., Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I., Perola M., Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N., Pare G., Oostra B.A., O'Donnell C.J., Nieminen M.S., Nickerson D.A., Montgomery G.W., Meitinger T., McPherson R., McCarthy M.I., McArdle W., Masson D., Martin N.G., Marroni F., Mangino M., Magnusson P.K., Lucas G., Luben R., Loos R.J., Lokki M.L., Lettre G., Langenberg C., Launer L.J., Lakatta E.G., Laaksonen R., Kyvik K.O., Kronenberg F., Konig I.R., Khaw K.T., Kaprio J., Kaplan L.M., Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E., Igl W., Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A., Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D., Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C., Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L., Erdmann J., Elliott P., Ejebe K.G., Doring A., Dominiczak A.F., Demissie S., Deloukas P., de Geus E.J., de Faire U., Crawford G., Collins F.S., Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P., Bonnycastle L.L., Boomsma D.I., Boekholdt S.M., Bergman R.N., Barroso I., Bandinelli S., Ballantyne C.M., Assimes T.L., Quertermous T., Altshuler D., Seielstad M., Wong T.Y., Tai E.S., Feranil A.B., Kuzawa C.W., Adair L.S., Taylor H.A. Jr., Borecki I.B., Gabriel S.B., Wilson J.G., Holm H., Thorsteinsdottir U., Gudnason V., Krauss R.M., Mohlke K.L., Ordovas J.M., Munroe P.B., Kooner J.S., Tall A.R., Hegele R.A., Kastelein J.J., Schadt E.E., Rotter J.I., Boerwinkle E., Strachan D.P., Mooser V., Stefansson K., Reilly M.P., Samani N.J., Schunkert H., Cupples L.A., Sandhu M.S., Ridker P.M., Rader D.J., van Duijn C.M., Peltonen L., Abecasis G.R., Boehnke M., Kathiresan S.
    Nature 466:707-713(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LDLCQ4, VARIANT ILE-98.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "A novel mutation of apolipoprotein B in a French Canadian family with homozygous hypobetalipoproteinemia."
    Gangloff A., Bergeron J., Couture P., Martins R., Hegele R.A., Gagne C.
    J. Clin. Lipidol. 5:414-417(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FHBL1.
  40. "Proprotein convertase subtilisin/kexin type 9 interacts with apolipoprotein B and prevents its intracellular degradation, irrespective of the low-density lipoprotein receptor."
    Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B.
    Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PCSK9.
  41. "Detection by denaturing gradient gel electrophoresis of a new polymorphism in the apolipoprotein B gene."
    Navajas M., Laurent A.-M., Moreel J.-F., Ragab A., Cambou J.-P., Cunny G., Cambien F., Roizes G.
    Hum. Genet. 86:91-93(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASN-4338.
  42. "Association between a specific apolipoprotein B mutation and familial defective apolipoprotein B-100."
    Soria L.F., Ludwig E.H., Clarke H.R.G., Vega G.L., Grundy S.M., McCarthy B.J.
    Proc. Natl. Acad. Sci. U.S.A. 86:587-591(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FDB GLN-3527.
  43. "Sequence polymorphism in the human apoB gene at position 8344."
    Huang L.-S., Gavish D., Breslow J.L.
    Nucleic Acids Res. 18:5922-5922(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-2739.
  44. "Familial ligand-defective apolipoprotein B. Identification of a new mutation that decreases LDL receptor binding affinity."
    Pullinger C.R., Hennessy L.K., Chatterton J.E., Liu W., Love J.A., Mendel C.M., Frost P.H., Malloy M.J., Schumaker V.N., Kane J.P.
    J. Clin. Invest. 95:1225-1234(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FDB CYS-3558.
  45. "Detection of new variants in the apolipoprotein B (Apo B) gene by PCR-SSCP."
    Poirier O., Ricard S., Behague I., Souriau C., Evans A.E., Arveiler D., Marques-Vidal P., Luc G., Roizes G., Cambien F.
    Hum. Mutat. 8:282-285(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LEU-1437; SER-1914; LYS-2566; THR-3121; ALA-3945; MET-4128 AND THR-4481.
  46. "Familial ligand-defective apolipoprotein B-100: simultaneous detection of the Arg3500-->Gln and Arg3531-->Cys mutations in a French population."
    Rabes J.P., Varret M., Saint-Jore B., Erlich D., Jondeau G., Krempf M., Giraudet P., Junien C., Boileau C.
    Hum. Mutat. 10:160-163(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FDB GLN-3527 AND CYS-3558.
  47. "Screening for mutations of the apolipoprotein B gene causing hypocholesterolemia."
    Leren T.P., Bakken K.S., Hoel V., Hjermann I., Berg K.
    Hum. Genet. 102:44-49(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-1914; ARG-1923; LEU-2739; HIS-3319; LYS-3427; GLU-3432 AND ILE-3921.
  48. "A novel nontruncating APOB gene mutation, R463W, causes familial hypobetalipoproteinemia."
    Burnett J.R., Shan J., Miskie B.A., Whitfield A.J., Yuan J., Tran K., McKnight C.J., Hegele R.A., Yao Z.
    J. Biol. Chem. 278:13442-13452(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FHBL1 TRP-490, VARIANT ILE-98, CHARACTERIZATION OF VARIANT TRP-490, MUTAGENESIS OF ASP-483 AND ARG-490.
  49. "Hypobetalipoproteinemia with an apparently recessive inheritance due to a 'de novo' mutation of apolipoprotein B."
    Lancellotti S., Di Leo E., Penacchioni J.Y., Balli F., Viola L., Bertolini S., Calandra S., Tarugi P.
    Biochim. Biophys. Acta 1688:61-67(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-1128.
  50. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-2564.
  51. "Molecular basis of autosomal dominant hypercholesterolemia: assessment in a large cohort of hypercholesterolemic children."
    van der Graaf A., Avis H.J., Kusters D.M., Vissers M.N., Hutten B.A., Defesche J.C., Huijgen R., Fouchier S.W., Wijburg F.A., Kastelein J.J., Wiegman A.
    Circulation 123:1167-1173(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FDB GLN-3527.
  52. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."
    Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
    J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLU-1218; ASP-1670; ASN-2037; CYS-2564 AND LYS-2566, IDENTIFICATION BY MASS SPECTROMETRY.
  53. "Genetic variation in APOB, PCSK9, and ANGPTL3 in carriers of pathogenic autosomal dominant hypercholesterolemic mutations with unexpected low LDL-Cl Levels."
    Huijgen R., Sjouke B., Vis K., de Randamie J.S., Defesche J.C., Kastelein J.J., Hovingh G.K., Fouchier S.W.
    Hum. Mutat. 33:448-455(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS 12-LEU--LEU-14 DEL; ILE-98; VAL-618; ILE-730; THR-1613; ARG-1923; LYS-2566; LEU-2739; GLN-3638; LEU-3835; LYS-4181; THR-4270; VAL-4314; ASN-4338; THR-4481 AND VAL-4482.

Entry informationi

Entry nameiAPOB_HUMAN
AccessioniPrimary (citable) accession number: P04114
Secondary accession number(s): O00502
, P78479, P78480, P78481, Q13779, Q13785, Q13786, Q13787, Q13788, Q4ZG63, Q53QC8, Q7Z600, Q9UMN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: July 13, 2010
Last modified: September 3, 2014
This is version 178 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

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