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Protein

Apolipoprotein B-100

Gene

APOB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • cholesterol transporter activity Source: BHF-UCL
  • heparin binding Source: BHF-UCL
  • lipase binding Source: BHF-UCL
  • low-density lipoprotein particle receptor binding Source: BHF-UCL
  • phospholipid binding Source: BHF-UCL

GO - Biological processi

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

BioCyciZFISH:ENSG00000084674-MONOMER.
ReactomeiR-HSA-171052. LDL-mediated lipid transport.
R-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-3000471. Scavenging by Class B Receptors.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-3000484. Scavenging by Class F Receptors.
R-HSA-3000497. Scavenging by Class H Receptors.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-5686938. Regulation of TLR by endogenous ligand.
R-HSA-8855121. VLDL interactions.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-8866423. VLDL biosynthesis.
R-HSA-975634. Retinoid metabolism and transport.
SIGNORiP04114.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:603. APOB.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • chylomicron Source: BHF-UCL
  • chylomicron remnant Source: BHF-UCL
  • clathrin-coated endocytic vesicle membrane Source: Reactome
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • early endosome Source: Reactome
  • endocytic vesicle lumen Source: Reactome
  • endoplasmic reticulum exit site Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • endosome lumen Source: Reactome
  • endosome membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • Golgi apparatus Source: HPA
  • intermediate-density lipoprotein particle Source: BHF-UCL
  • intracellular membrane-bounded organelle Source: ProtInc
  • low-density lipoprotein particle Source: BHF-UCL
  • mature chylomicron Source: BHF-UCL
  • neuronal cell body Source: MGI
  • plasma membrane Source: HPA
  • 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)3 Publications
The disease is caused by mutations affecting the gene represented in this entry. Most cases of FHBL1 result from nonsense mutations in the APOB gene that lead to a premature stop codon, which generate prematurely truncated apo B protein products (PubMed:21981844).1 Publication
Disease descriptionA disorder of lipid metabolism characterized by less than 5th percentile age- and sex-specific levels of low density lipoproteins, and dietary fat malabsorption. Clinical presentation may vary from no symptoms to severe gastrointestinal and neurological dysfunction similar to abetalipoproteinemia.
See also OMIM:615558
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022610490R → W in FHBL1; reduced protein secretion. 1 Publication1
Natural variantiVAR_076539952V → L in FHBL1; unknown pathological significance; does not affect interaction with MTTP. 1 Publication1
Familial ligand-defective apolipoprotein B-100 (FDB)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionDominantly 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.
See also OMIM:144010
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0050253527R → Q in FDB. 3 PublicationsCorresponds to variant rs5742904dbSNPEnsembl.1
Natural variantiVAR_0050263558R → C in FDB. 2 PublicationsCorresponds to variant rs12713559dbSNPEnsembl.1

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi483D → N: Impairs protein secretion. 1 Publication1
Mutagenesisi483D → Q: Does not affect protein secretion. 1 Publication1
Mutagenesisi490R → A: Impairs protein secretion. 1 Publication1
Mutagenesisi490R → K: Does not affect protein secretion. 1 Publication1

Keywords - Diseasei

Atherosclerosis, Disease mutation

Organism-specific databases

DisGeNETi338.
MalaCardsiAPOB.
MIMi107730. gene+phenotype.
144010. phenotype.
615558. phenotype.
Orphaneti426. Familial hypobetalipoproteinemia.
406. Heterozygous familial hypercholesterolemia.
391665. Homozygous familial hypercholesterolemia.
PharmGKBiPA50.

Chemistry databases

ChEMBLiCHEMBL4549.

Polymorphism and mutation databases

BioMutaiAPOB.
DMDMi300669605.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000002075028 – 4563Apolipoprotein B-100Add BLAST4536
ChainiPRO_000002075128 – 2179Apolipoprotein B-48Add BLAST2152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi34N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi39 ↔ 88PROSITE-ProRule annotation1 Publication
Disulfide bondi78 ↔ 97PROSITE-ProRule annotation1 Publication
Glycosylationi185N-linked (GlcNAc...)1 Publication1
Disulfide bondi186 ↔ 212PROSITE-ProRule annotation1 Publication
Disulfide bondi245 ↔ 261PROSITE-ProRule annotation1 Publication
Disulfide bondi385 ↔ 390PROSITE-ProRule annotation1 Publication
Disulfide bondi478 ↔ 513PROSITE-ProRule annotation1 Publication
Disulfide bondi966 ↔ 976PROSITE-ProRule annotation1 Publication
Glycosylationi983N-linked (GlcNAc...)Sequence analysis1
Lipidationi1112S-palmitoyl cysteine1 Publication1
Glycosylationi1368N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1377N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1523N-linked (GlcNAc...)2 Publications1
Modified residuei2004N6-acetyllysineCombined sources1
Glycosylationi2239N-linked (GlcNAc...)1 Publication1
Glycosylationi2560N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2779N-linked (GlcNAc...)1 Publication1
Glycosylationi2982N-linked (GlcNAc...)2 Publications1
Glycosylationi3101N-linked (GlcNAc...)1 Publication1
Disulfide bondi3194 ↔ 3324PROSITE-ProRule annotation1 Publication
Glycosylationi3224N-linked (GlcNAc...)1 Publication1
Modified residuei3279PhosphoserineCombined sources1
Glycosylationi3336N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3358N-linked (GlcNAc...)1 Publication1
Glycosylationi3411N-linked (GlcNAc...)1 Publication1
Glycosylationi3465N-linked (GlcNAc...)2 Publications1
Glycosylationi3895N-linked (GlcNAc...)2 Publications1
Modified residuei4048Phosphoserine; by FAM20CCombined sources1 Publication1
Modified residuei4052PhosphothreonineCombined sources1
Glycosylationi4237N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4431N-linked (GlcNAc...)Sequence analysis1

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, Phosphoprotein

Proteomic databases

EPDiP04114.
MaxQBiP04114.
PaxDbiP04114.
PeptideAtlasiP04114.
PRIDEiP04114.

PTM databases

iPTMnetiP04114.
PhosphoSitePlusiP04114.
SwissPalmiP04114.
UniCarbKBiP04114.

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSG00000084674.
ExpressionAtlasiP04114. baseline and differential.
GenevisibleiP04114. HS.

Organism-specific databases

HPAiCAB016070.
HPA049793.

Interactioni

Subunit structurei

Interacts with PCSK9 (PubMed:22580899). Interacts with MTTP (PubMed:26224785, PubMed:27206948).3 Publications

Binary interactionsi

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

GO - Molecular functioni

  • lipase binding Source: BHF-UCL
  • low-density lipoprotein particle receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106835. 64 interactors.
DIPiDIP-44767N.
IntActiP04114. 30 interactors.
MINTiMINT-1506918.
STRINGi9606.ENSP00000233242.

Chemistry databases

BindingDBiP04114.

Structurei

3D structure databases

ProteinModelPortaliP04114.
SMRiP04114.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 672VitellogeninPROSITE-ProRule annotationAdd BLAST627

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 126Heparin-bindingAdd BLAST95
Regioni232 – 306Heparin-bindingAdd BLAST75
Regioni902 – 959Heparin-bindingAdd BLAST58
Regioni2043 – 2178Heparin-bindingAdd BLAST136
Regioni3161 – 3236Heparin-bindingAdd BLAST76
Regioni3174 – 3184Basic (possible receptor binding region)Add BLAST11
Regioni3373 – 3393LDL receptor bindingAdd BLAST21
Regioni3383 – 3516Heparin-bindingAdd BLAST134
Regioni3386 – 3394Basic (possible receptor binding region)9

Sequence similaritiesi

Contains 1 vitellogenin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4338. Eukaryota.
ENOG411104F. LUCA.
HOVERGENiHBG050546.
InParanoidiP04114.
KOiK14462.
OrthoDBiEOG091G000G.
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]
SMARTiSM01169. DUF1943. 1 hit.
SM00638. 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

« Hide

        10         20         30         40         50
MDPPRPALLA LLALPALLLL LLAGARAEEE MLENVSLVCP KDATRFKHLR
60 70 80 90 100
KYTYNYEAES SSGVPGTADS RSATRINCKV ELEVPQLCSF ILKTSQCTLK
110 120 130 140 150
EVYGFNPEGK ALLKKTKNSE EFAAAMSRYE LKLAIPEGKQ VFLYPEKDEP
160 170 180 190 200
TYILNIKRGI ISALLVPPET EEAKQVLFLD TVYGNCSTHF TVKTRKGNVA
210 220 230 240 250
TEISTERDLG QCDRFKPIRT GISPLALIKG MTRPLSTLIS SSQSCQYTLD
260 270 280 290 300
AKRKHVAEAI CKEQHLFLPF SYKNKYGMVA QVTQTLKLED TPKINSRFFG
310 320 330 340 350
EGTKKMGLAF ESTKSTSPPK QAEAVLKTLQ ELKKLTISEQ NIQRANLFNK
360 370 380 390 400
LVTELRGLSD EAVTSLLPQL IEVSSPITLQ ALVQCGQPQC STHILQWLKR
410 420 430 440 450
VHANPLLIDV VTYLVALIPE PSAQQLREIF NMARDQRSRA TLYALSHAVN
460 470 480 490 500
NYHKTNPTGT QELLDIANYL MEQIQDDCTG DEDYTYLILR VIGNMGQTME
510 520 530 540 550
QLTPELKSSI LKCVQSTKPS LMIQKAAIQA LRKMEPKDKD QEVLLQTFLD
560 570 580 590 600
DASPGDKRLA AYLMLMRSPS QADINKIVQI LPWEQNEQVK NFVASHIANI
610 620 630 640 650
LNSEELDIQD LKKLVKEALK ESQLPTVMDF RKFSRNYQLY KSVSLPSLDP
660 670 680 690 700
ASAKIEGNLI FDPNNYLPKE SMLKTTLTAF GFASADLIEI GLEGKGFEPT
710 720 730 740 750
LEALFGKQGF FPDSVNKALY WVNGQVPDGV SKVLVDHFGY TKDDKHEQDM
760 770 780 790 800
VNGIMLSVEK LIKDLKSKEV PEARAYLRIL GEELGFASLH DLQLLGKLLL
810 820 830 840 850
MGARTLQGIP QMIGEVIRKG SKNDFFLHYI FMENAFELPT GAGLQLQISS
860 870 880 890 900
SGVIAPGAKA GVKLEVANMQ AELVAKPSVS VEFVTNMGII IPDFARSGVQ
910 920 930 940 950
MNTNFFHESG LEAHVALKAG KLKFIIPSPK RPVKLLSGGN TLHLVSTTKT
960 970 980 990 1000
EVIPPLIENR QSWSVCKQVF PGLNYCTSGA YSNASSTDSA SYYPLTGDTR
1010 1020 1030 1040 1050
LELELRPTGE IEQYSVSATY ELQREDRALV DTLKFVTQAE GAKQTEATMT
1060 1070 1080 1090 1100
FKYNRQSMTL SSEVQIPDFD VDLGTILRVN DESTEGKTSY RLTLDIQNKK
1110 1120 1130 1140 1150
ITEVALMGHL SCDTKEERKI KGVISIPRLQ AEARSEILAH WSPAKLLLQM
1160 1170 1180 1190 1200
DSSATAYGST VSKRVAWHYD EEKIEFEWNT GTNVDTKKMT SNFPVDLSDY
1210 1220 1230 1240 1250
PKSLHMYANR LLDHRVPQTD MTFRHVGSKL IVAMSSWLQK ASGSLPYTQT
1260 1270 1280 1290 1300
LQDHLNSLKE FNLQNMGLPD FHIPENLFLK SDGRVKYTLN KNSLKIEIPL
1310 1320 1330 1340 1350
PFGGKSSRDL KMLETVRTPA LHFKSVGFHL PSREFQVPTF TIPKLYQLQV
1360 1370 1380 1390 1400
PLLGVLDLST NVYSNLYNWS ASYSGGNTST DHFSLRARYH MKADSVVDLL
1410 1420 1430 1440 1450
SYNVQGSGET TYDHKNTFTL SYDGSLRHKF LDSNIKFSHV EKLGNNPVSK
1460 1470 1480 1490 1500
GLLIFDASSS WGPQMSASVH LDSKKKQHLF VKEVKIDGQF RVSSFYAKGT
1510 1520 1530 1540 1550
YGLSCQRDPN TGRLNGESNL RFNSSYLQGT NQITGRYEDG TLSLTSTSDL
1560 1570 1580 1590 1600
QSGIIKNTAS LKYENYELTL KSDTNGKYKN FATSNKMDMT FSKQNALLRS
1610 1620 1630 1640 1650
EYQADYESLR FFSLLSGSLN SHGLELNADI LGTDKINSGA HKATLRIGQD
1660 1670 1680 1690 1700
GISTSATTNL KCSLLVLENE LNAELGLSGA SMKLTTNGRF REHNAKFSLD
1710 1720 1730 1740 1750
GKAALTELSL GSAYQAMILG VDSKNIFNFK VSQEGLKLSN DMMGSYAEMK
1760 1770 1780 1790 1800
FDHTNSLNIA GLSLDFSSKL DNIYSSDKFY KQTVNLQLQP YSLVTTLNSD
1810 1820 1830 1840 1850
LKYNALDLTN NGKLRLEPLK LHVAGNLKGA YQNNEIKHIY AISSAALSAS
1860 1870 1880 1890 1900
YKADTVAKVQ GVEFSHRLNT DIAGLASAID MSTNYNSDSL HFSNVFRSVM
1910 1920 1930 1940 1950
APFTMTIDAH TNGNGKLALW GEHTGQLYSK FLLKAEPLAF TFSHDYKGST
1960 1970 1980 1990 2000
SHHLVSRKSI SAALEHKVSA LLTPAEQTGT WKLKTQFNNN EYSQDLDAYN
2010 2020 2030 2040 2050
TKDKIGVELT GRTLADLTLL DSPIKVPLLL SEPINIIDAL EMRDAVEKPQ
2060 2070 2080 2090 2100
EFTIVAFVKY DKNQDVHSIN LPFFETLQEY FERNRQTIIV VLENVQRNLK
2110 2120 2130 2140 2150
HINIDQFVRK YRAALGKLPQ QANDYLNSFN WERQVSHAKE KLTALTKKYR
2160 2170 2180 2190 2200
ITENDIQIAL DDAKINFNEK LSQLQTYMIQ FDQYIKDSYD LHDLKIAIAN
2210 2220 2230 2240 2250
IIDEIIEKLK SLDEHYHIRV NLVKTIHDLH LFIENIDFNK SGSSTASWIQ
2260 2270 2280 2290 2300
NVDTKYQIRI QIQEKLQQLK RHIQNIDIQH LAGKLKQHIE AIDVRVLLDQ
2310 2320 2330 2340 2350
LGTTISFERI NDILEHVKHF VINLIGDFEV AEKINAFRAK VHELIERYEV
2360 2370 2380 2390 2400
DQQIQVLMDK LVELAHQYKL KETIQKLSNV LQQVKIKDYF EKLVGFIDDA
2410 2420 2430 2440 2450
VKKLNELSFK TFIEDVNKFL DMLIKKLKSF DYHQFVDETN DKIREVTQRL
2460 2470 2480 2490 2500
NGEIQALELP QKAEALKLFL EETKATVAVY LESLQDTKIT LIINWLQEAL
2510 2520 2530 2540 2550
SSASLAHMKA KFRETLEDTR DRMYQMDIQQ ELQRYLSLVG QVYSTLVTYI
2560 2570 2580 2590 2600
SDWWTLAAKN LTDFAEQYSI QDWAKRMKAL VEQGFTVPEI KTILGTMPAF
2610 2620 2630 2640 2650
EVSLQALQKA TFQTPDFIVP LTDLRIPSVQ INFKDLKNIK IPSRFSTPEF
2660 2670 2680 2690 2700
TILNTFHIPS FTIDFVEMKV KIIRTIDQML NSELQWPVPD IYLRDLKVED
2710 2720 2730 2740 2750
IPLARITLPD FRLPEIAIPE FIIPTLNLND FQVPDLHIPE FQLPHISHTI
2760 2770 2780 2790 2800
EVPTFGKLYS ILKIQSPLFT LDANADIGNG TTSANEAGIA ASITAKGESK
2810 2820 2830 2840 2850
LEVLNFDFQA NAQLSNPKIN PLALKESVKF SSKYLRTEHG SEMLFFGNAI
2860 2870 2880 2890 2900
EGKSNTVASL HTEKNTLELS NGVIVKINNQ LTLDSNTKYF HKLNIPKLDF
2910 2920 2930 2940 2950
SSQADLRNEI KTLLKAGHIA WTSSGKGSWK WACPRFSDEG THESQISFTI
2960 2970 2980 2990 3000
EGPLTSFGLS NKINSKHLRV NQNLVYESGS LNFSKLEIQS QVDSQHVGHS
3010 3020 3030 3040 3050
VLTAKGMALF GEGKAEFTGR HDAHLNGKVI GTLKNSLFFS AQPFEITAST
3060 3070 3080 3090 3100
NNEGNLKVRF PLRLTGKIDF LNNYALFLSP SAQQASWQVS ARFNQYKYNQ
3110 3120 3130 3140 3150
NFSAGNNENI MEAHVGINGE ANLDFLNIPL TIPEMRLPYT IITTPPLKDF
3160 3170 3180 3190 3200
SLWEKTGLKE FLKTTKQSFD LSVKAQYKKN KHRHSITNPL AVLCEFISQS
3210 3220 3230 3240 3250
IKSFDRHFEK NRNNALDFVT KSYNETKIKF DKYKAEKSHD ELPRTFQIPG
3260 3270 3280 3290 3300
YTVPVVNVEV SPFTIEMSAF GYVFPKAVSM PSFSILGSDV RVPSYTLILP
3310 3320 3330 3340 3350
SLELPVLHVP RNLKLSLPDF KELCTISHIF IPAMGNITYD FSFKSSVITL
3360 3370 3380 3390 3400
NTNAELFNQS DIVAHLLSSS SSVIDALQYK LEGTTRLTRK RGLKLATALS
3410 3420 3430 3440 3450
LSNKFVEGSH NSTVSLTTKN MEVSVATTTK AQIPILRMNF KQELNGNTKS
3460 3470 3480 3490 3500
KPTVSSSMEF KYDFNSSMLY STAKGAVDHK LSLESLTSYF SIESSTKGDV
3510 3520 3530 3540 3550
KGSVLSREYS GTIASEANTY LNSKSTRSSV KLQGTSKIDD IWNLEVKENF
3560 3570 3580 3590 3600
AGEATLQRIY SLWEHSTKNH LQLEGLFFTN GEHTSKATLE LSPWQMSALV
3610 3620 3630 3640 3650
QVHASQPSSF HDFPDLGQEV ALNANTKNQK IRWKNEVRIH SGSFQSQVEL
3660 3670 3680 3690 3700
SNDQEKAHLD IAGSLEGHLR FLKNIILPVY DKSLWDFLKL DVTTSIGRRQ
3710 3720 3730 3740 3750
HLRVSTAFVY TKNPNGYSFS IPVKVLADKF IIPGLKLNDL NSVLVMPTFH
3760 3770 3780 3790 3800
VPFTDLQVPS CKLDFREIQI YKKLRTSSFA LNLPTLPEVK FPEVDVLTKY
3810 3820 3830 3840 3850
SQPEDSLIPF FEITVPESQL TVSQFTLPKS VSDGIAALDL NAVANKIADF
3860 3870 3880 3890 3900
ELPTIIVPEQ TIEIPSIKFS VPAGIVIPSF QALTARFEVD SPVYNATWSA
3910 3920 3930 3940 3950
SLKNKADYVE TVLDSTCSST VQFLEYELNV LGTHKIEDGT LASKTKGTFA
3960 3970 3980 3990 4000
HRDFSAEYEE DGKYEGLQEW EGKAHLNIKS PAFTDLHLRY QKDKKGISTS
4010 4020 4030 4040 4050
AASPAVGTVG MDMDEDDDFS KWNFYYSPQS SPDKKLTIFK TELRVRESDE
4060 4070 4080 4090 4100
ETQIKVNWEE EAASGLLTSL KDNVPKATGV LYDYVNKYHW EHTGLTLREV
4110 4120 4130 4140 4150
SSKLRRNLQN NAEWVYQGAI RQIDDIDVRF QKAASGTTGT YQEWKDKAQN
4160 4170 4180 4190 4200
LYQELLTQEG QASFQGLKDN VFDGLVRVTQ EFHMKVKHLI DSLIDFLNFP
4210 4220 4230 4240 4250
RFQFPGKPGI YTREELCTMF IREVGTVLSQ VYSKVHNGSE ILFSYFQDLV
4260 4270 4280 4290 4300
ITLPFELRKH KLIDVISMYR ELLKDLSKEA QEVFKAIQSL KTTEVLRNLQ
4310 4320 4330 4340 4350
DLLQFIFQLI EDNIKQLKEM KFTYLINYIQ DEINTIFSDY IPYVFKLLKE
4360 4370 4380 4390 4400
NLCLNLHKFN EFIQNELQEA SQELQQIHQY IMALREEYFD PSIVGWTVKY
4410 4420 4430 4440 4450
YELEEKIVSL IKNLLVALKD FHSEYIVSAS NFTSQLSSQV EQFLHRNIQE
4460 4470 4480 4490 4500
YLSILTDPDG KGKEKIAELS ATAQEIIKSQ AIATKKIISD YHQQFRYKLQ
4510 4520 4530 4540 4550
DFSDQLSDYY EKFIAESKRL IDLSIQNYHT FLIYITELLK KLQSTTVMNP
4560
YMKLAPGELT IIL
Length:4,563
Mass (Da):515,605
Last modified:July 13, 2010 - v2
Checksum:i6800F94BF6ADF698
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11 – 13Missing in AAB60718 (PubMed:3030729).Curated3
Sequence conflicti11 – 13Missing in CAA28420 (PubMed:3030729).Curated3
Sequence conflicti329L → V in AAA35549 (PubMed:3759943).Curated1
Sequence conflicti645L → I in AAA35549 (PubMed:3759943).Curated1
Sequence conflicti704L → P in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti792 – 809LQLLG…TLQGI → SSSWKAASHGCPHSAGD in AAA51759 (PubMed:3860836).CuratedAdd BLAST18
Sequence conflicti793Q → R in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti893D → K AA sequence (PubMed:6373369).Curated1
Sequence conflicti919A → P in AAA35549 (PubMed:3759943).Curated1
Sequence conflicti1109H → D in CAA28420 (PubMed:3030729).Curated1
Sequence conflicti1180T → R in AAA51752 (PubMed:3461454).Curated1
Sequence conflicti1271F → S in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti1418F → S in CAA28420 (PubMed:3030729).Curated1
Sequence conflicti1445N → I in AAA51752 (PubMed:3461454).Curated1
Sequence conflicti1535G → E in AAA51752 (PubMed:3461454).Curated1
Sequence conflicti1867R → G in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti2098N → K in CAA28420 (PubMed:3030729).Curated1
Sequence conflicti2218I → T in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti2221N → I in CAA28420 (PubMed:3030729).Curated1
Sequence conflicti2324 – 2326LIG → PYW in AAA51741 (PubMed:3676265).Curated3
Sequence conflicti2353Q → H in AAA51741 (PubMed:3676265).Curated1
Sequence conflicti2540G → S in CAA28420 (PubMed:3030729).Curated1
Sequence conflicti2718 – 2737Missing in AAA51758 (PubMed:2883086).CuratedAdd BLAST20
Sequence conflicti2933C → S in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti3114H → L AA sequence (PubMed:6373369).Curated1
Sequence conflicti3131T → R AA sequence (PubMed:6373369).Curated1
Sequence conflicti3134E → P AA sequence (PubMed:6373369).Curated1
Sequence conflicti3137L → R AA sequence (PubMed:6373369).Curated1
Sequence conflicti3239H → Q in CAA28420 (PubMed:3030729).Curated1
Sequence conflicti3286L → I in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti3291R → L in AAA51758 (PubMed:2883086).Curated1
Sequence conflicti3337I → N in AAA51758 (PubMed:2883086).Curated1
Sequence conflicti3431A → P in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti3728D → N in AAA51742 (PubMed:2932736).Curated1
Sequence conflicti3782N → T in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti3824Q → R in CAA28420 (PubMed:3030729).Curated1
Sequence conflicti3824Q → R in AAA51750 (PubMed:2994225).Curated1
Sequence conflicti3876V → A in AAA35549 (PubMed:3759943).Curated1
Sequence conflicti3876V → A in AAA51742 (PubMed:2932736).Curated1
Sequence conflicti3911T → Y AA sequence (PubMed:2115173).Curated1
Sequence conflicti3983F → S in AAA51742 (PubMed:2932736).Curated1
Sequence conflicti4002A → P in AAA51742 (PubMed:2932736).Curated1
Sequence conflicti4110 – 4111NN → DH in AAA35549 (PubMed:3759943).Curated2
Sequence conflicti4110 – 4111NN → DH in AAA51742 (PubMed:2932736).Curated2
Sequence conflicti4122Q → E in AAA35549 (PubMed:3759943).Curated1
Sequence conflicti4122Q → E in AAA51742 (PubMed:2932736).Curated1
Sequence conflicti4128V → E in AAA35549 (PubMed:3759943).Curated1
Sequence conflicti4128V → E in AAA51742 (PubMed:2932736).Curated1
Sequence conflicti4133A → G in AAA35549 (PubMed:3759943).Curated1
Sequence conflicti4133A → G in AAA51742 (PubMed:2932736).Curated1
Sequence conflicti4188H → K in AAB04636 (PubMed:3464946).Curated1
Sequence conflicti4217 – 4218CT → FP in AAA35548 (PubMed:3024665).Curated2
Sequence conflicti4221I → M in AAB04636 (PubMed:3464946).Curated1

RNA editingi

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

Polymorphismi

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06727712 – 14Missing .1 Publication3
Natural variantiVAR_01618498T → I Polymorphism that influences plasma concentrations of low density lipoprotein cholesterol. 6 PublicationsCorresponds to variant rs1367117dbSNPEnsembl.1
Natural variantiVAR_022036103Y → H.Corresponds to variant rs9282603dbSNPEnsembl.1
Natural variantiVAR_022037145P → S.Corresponds to variant rs6752026dbSNPEnsembl.1
Natural variantiVAR_056737194T → M.Corresponds to variant rs13306198dbSNPEnsembl.1
Natural variantiVAR_076538251A → T Polymorphism; does not affect plasma lipid levels. 1 PublicationCorresponds to variant rs61741625dbSNPEnsembl.1
Natural variantiVAR_019827273K → N.1 PublicationCorresponds to variant rs1126419dbSNPEnsembl.1
Natural variantiVAR_029341408I → T.Corresponds to variant rs12714225dbSNPEnsembl.1
Natural variantiVAR_022610490R → W in FHBL1; reduced protein secretion. 1 Publication1
Natural variantiVAR_020135554P → L.Corresponds to variant rs12714214dbSNPEnsembl.1
Natural variantiVAR_019828618A → V.3 PublicationsCorresponds to variant rs679899dbSNPEnsembl.1
Natural variantiVAR_020136730V → I.1 PublicationCorresponds to variant rs12691202dbSNPEnsembl.1
Natural variantiVAR_016185733V → I.Corresponds to variant rs1800476dbSNPEnsembl.1
Natural variantiVAR_020137741T → N.Corresponds to variant rs12714192dbSNPEnsembl.1
Natural variantiVAR_029342877P → L.Corresponds to variant rs12714097dbSNPEnsembl.1
Natural variantiVAR_076539952V → L in FHBL1; unknown pathological significance; does not affect interaction with MTTP. 1 Publication1
Natural variantiVAR_056738955P → S.Corresponds to variant rs13306206dbSNPEnsembl.1
Natural variantiVAR_0293431086G → S.Corresponds to variant rs12720801dbSNPEnsembl.1
Natural variantiVAR_0293441113D → H.Corresponds to variant rs12713844dbSNPEnsembl.1
Natural variantiVAR_0226111128R → H.1 PublicationCorresponds to variant rs12713843dbSNPEnsembl.1
Natural variantiVAR_0198291218Q → E Polymorphism; confirmed at protein level. 2 PublicationsCorresponds to variant rs1041956dbSNPEnsembl.1
Natural variantiVAR_0293451388R → H.Corresponds to variant rs13306187dbSNPEnsembl.1
Natural variantiVAR_0615581422Y → C.8 PublicationsCorresponds to variant rs568413dbSNPEnsembl.1
Natural variantiVAR_0050161437F → L.1 PublicationCorresponds to variant rs1801697dbSNPEnsembl.1
Natural variantiVAR_0672781613S → T.1 Publication1
Natural variantiVAR_0689111670E → D Polymorphism; confirmed at protein level. 2 Publications1
Natural variantiVAR_0050171914N → S.2 PublicationsCorresponds to variant rs1801699dbSNPEnsembl.1
Natural variantiVAR_0050181923H → R.2 PublicationsCorresponds to variant rs533617dbSNPEnsembl.1
Natural variantiVAR_0689122037I → N Polymorphism; confirmed at protein level. 2 Publications1
Natural variantiVAR_0198302092L → V.1 PublicationCorresponds to variant rs1041960dbSNPEnsembl.1
Natural variantiVAR_0293462299D → H.Corresponds to variant rs12713681dbSNPEnsembl.1
Natural variantiVAR_0595822313I → V.8 PublicationsCorresponds to variant rs584542dbSNPEnsembl.1
Natural variantiVAR_0198312365A → T.1 PublicationCorresponds to variant rs1041971dbSNPEnsembl.1
Natural variantiVAR_0201382456A → D.Corresponds to variant rs12713675dbSNPEnsembl.1
Natural variantiVAR_0357952564F → C in a colorectal cancer sample; somatic mutation; confirmed at protein level. 2 Publications1
Natural variantiVAR_0050192566E → K Polymorphism; confirmed at protein level. 3 PublicationsCorresponds to variant rs1801696dbSNPEnsembl.1
Natural variantiVAR_0198322680L → Q.1 PublicationCorresponds to variant rs1042013dbSNPEnsembl.1
Natural variantiVAR_0050202739P → L.3 PublicationsCorresponds to variant rs676210dbSNPEnsembl.1
Natural variantiVAR_0220382785N → H.Corresponds to variant rs2163204dbSNPEnsembl.1
Natural variantiVAR_0050213121A → T.1 PublicationCorresponds to variant rs1801694dbSNPEnsembl.1
Natural variantiVAR_0293473182H → N.Corresponds to variant rs12720848dbSNPEnsembl.1
Natural variantiVAR_0293483279S → G.Corresponds to variant rs12720854dbSNPEnsembl.1
Natural variantiVAR_0201393294S → P.Corresponds to variant rs12720855dbSNPEnsembl.1
Natural variantiVAR_0050223319D → H.8 Publications1
Natural variantiVAR_0050233427T → K.8 Publications1
Natural variantiVAR_0050243432Q → E.8 PublicationsCorresponds to variant rs1042023dbSNPEnsembl.1
Natural variantiVAR_0050253527R → Q in FDB. 3 PublicationsCorresponds to variant rs5742904dbSNPEnsembl.1
Natural variantiVAR_0050263558R → C in FDB. 2 PublicationsCorresponds to variant rs12713559dbSNPEnsembl.1
Natural variantiVAR_0161863638R → Q.1 PublicationCorresponds to variant rs1801701dbSNPEnsembl.1
Natural variantiVAR_0198333732I → T.4 PublicationsCorresponds to variant rs1042025dbSNPEnsembl.1
Natural variantiVAR_0293493801S → T.Corresponds to variant rs12713540dbSNPEnsembl.1
Natural variantiVAR_0672793835I → L.1 Publication1
Natural variantiVAR_0050273921V → I.1 PublicationCorresponds to variant rs72654409dbSNPEnsembl.1
Natural variantiVAR_0050283945T → A.1 PublicationCorresponds to variant rs1801698dbSNPEnsembl.1
Natural variantiVAR_0198343949F → L.5 PublicationsCorresponds to variant rs1042027dbSNPEnsembl.1
Natural variantiVAR_0198353964Y → F.4 PublicationsCorresponds to variant rs1126468dbSNPEnsembl.1
Natural variantiVAR_0050294128V → M.1 PublicationCorresponds to variant rs1801703dbSNPEnsembl.1
Natural variantiVAR_0161874181E → K.6 PublicationsCorresponds to variant rs1042031dbSNPEnsembl.1
Natural variantiVAR_0161884270R → T.1 PublicationCorresponds to variant rs1801702dbSNPEnsembl.1
Natural variantiVAR_0672804314I → V.1 PublicationCorresponds to variant rs72654423dbSNPEnsembl.1
Natural variantiVAR_0050304338S → N.11 PublicationsCorresponds to variant rs1042034dbSNPEnsembl.1
Natural variantiVAR_0293504394V → A.Corresponds to variant rs12720843dbSNPEnsembl.1
Natural variantiVAR_0050314481A → T.2 PublicationsCorresponds to variant rs1801695dbSNPEnsembl.1
Natural variantiVAR_0672814482I → V.1 Publication1
Natural variantiVAR_0201404484T → M.Corresponds to variant rs12713450dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04506 mRNA. Translation: CAA28191.1.
M19828
, M19808, M19809, M19810, M19811, M19812, M19813, M19815, M19816, M19818, M19820, M19821, M19823, M19824, M19825, M19827 Genomic DNA. Translation: AAB00481.1.
J02610 mRNA. Translation: AAA35549.1.
M14162 mRNA. Translation: AAB04636.1.
M15053 Genomic DNA. Translation: AAB60718.1.
X04714 mRNA. Translation: CAA28420.1.
AY324608 Genomic DNA. Translation: AAP72970.1.
AC010872 Genomic DNA. Translation: AAX88848.1.
AC115619 Genomic DNA. Translation: AAX93246.1.
M14081 mRNA. Translation: AAA51752.1. Frameshift.
M12681 mRNA. Translation: AAA51753.1.
M12480 mRNA. Translation: AAA51751.1.
K03175 mRNA. Translation: AAA51759.1.
M15421 mRNA. Translation: AAA51758.1.
M17367 mRNA. Translation: AAA51741.1.
M31030 mRNA. Translation: AAA51756.1.
X03325 mRNA. Translation: CAA27044.1.
X03326 mRNA. Translation: CAA27045.1.
M17779 mRNA. Translation: AAA51755.1.
M19734 mRNA. Translation: AAA35544.1.
M18471 mRNA. Translation: AAA35541.1.
X03045 mRNA. Translation: CAA26850.1.
M10374 mRNA. Translation: AAA51750.1.
M12413 mRNA. Translation: AAA51742.1.
M36676 mRNA. Translation: AAA35548.1.
CCDSiCCDS1703.1.
PIRiA27850. LPHUB.
RefSeqiNP_000375.2. NM_000384.2.
UniGeneiHs.120759.

Genome annotation databases

EnsembliENST00000233242; ENSP00000233242; ENSG00000084674.
GeneIDi338.
KEGGihsa:338.
UCSCiuc002red.3. human.

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:
EMBLi
GenBanki
DDBJi
Links Updated
X04506 mRNA. Translation: CAA28191.1.
M19828
, M19808, M19809, M19810, M19811, M19812, M19813, M19815, M19816, M19818, M19820, M19821, M19823, M19824, M19825, M19827 Genomic DNA. Translation: AAB00481.1.
J02610 mRNA. Translation: AAA35549.1.
M14162 mRNA. Translation: AAB04636.1.
M15053 Genomic DNA. Translation: AAB60718.1.
X04714 mRNA. Translation: CAA28420.1.
AY324608 Genomic DNA. Translation: AAP72970.1.
AC010872 Genomic DNA. Translation: AAX88848.1.
AC115619 Genomic DNA. Translation: AAX93246.1.
M14081 mRNA. Translation: AAA51752.1. Frameshift.
M12681 mRNA. Translation: AAA51753.1.
M12480 mRNA. Translation: AAA51751.1.
K03175 mRNA. Translation: AAA51759.1.
M15421 mRNA. Translation: AAA51758.1.
M17367 mRNA. Translation: AAA51741.1.
M31030 mRNA. Translation: AAA51756.1.
X03325 mRNA. Translation: CAA27044.1.
X03326 mRNA. Translation: CAA27045.1.
M17779 mRNA. Translation: AAA51755.1.
M19734 mRNA. Translation: AAA35544.1.
M18471 mRNA. Translation: AAA35541.1.
X03045 mRNA. Translation: CAA26850.1.
M10374 mRNA. Translation: AAA51750.1.
M12413 mRNA. Translation: AAA51742.1.
M36676 mRNA. Translation: AAA35548.1.
CCDSiCCDS1703.1.
PIRiA27850. LPHUB.
RefSeqiNP_000375.2. NM_000384.2.
UniGeneiHs.120759.

3D structure databases

ProteinModelPortaliP04114.
SMRiP04114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106835. 64 interactors.
DIPiDIP-44767N.
IntActiP04114. 30 interactors.
MINTiMINT-1506918.
STRINGi9606.ENSP00000233242.

Chemistry databases

BindingDBiP04114.
ChEMBLiCHEMBL4549.

PTM databases

iPTMnetiP04114.
PhosphoSitePlusiP04114.
SwissPalmiP04114.
UniCarbKBiP04114.

Polymorphism and mutation databases

BioMutaiAPOB.
DMDMi300669605.

Proteomic databases

EPDiP04114.
MaxQBiP04114.
PaxDbiP04114.
PeptideAtlasiP04114.
PRIDEiP04114.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233242; ENSP00000233242; ENSG00000084674.
GeneIDi338.
KEGGihsa:338.
UCSCiuc002red.3. human.

Organism-specific databases

CTDi338.
DisGeNETi338.
GeneCardsiAPOB.
GeneReviewsiAPOB.
H-InvDBHIX0024005.
HGNCiHGNC:603. APOB.
HPAiCAB016070.
HPA049793.
MalaCardsiAPOB.
MIMi107730. gene+phenotype.
144010. phenotype.
615558. phenotype.
neXtProtiNX_P04114.
Orphaneti426. Familial hypobetalipoproteinemia.
406. Heterozygous familial hypercholesterolemia.
391665. Homozygous familial hypercholesterolemia.
PharmGKBiPA50.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4338. Eukaryota.
ENOG411104F. LUCA.
HOVERGENiHBG050546.
InParanoidiP04114.
KOiK14462.
OrthoDBiEOG091G000G.
PhylomeDBiP04114.
TreeFamiTF331316.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000084674-MONOMER.
ReactomeiR-HSA-171052. LDL-mediated lipid transport.
R-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-3000471. Scavenging by Class B Receptors.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-3000484. Scavenging by Class F Receptors.
R-HSA-3000497. Scavenging by Class H Receptors.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-5686938. Regulation of TLR by endogenous ligand.
R-HSA-8855121. VLDL interactions.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-8866423. VLDL biosynthesis.
R-HSA-975634. Retinoid metabolism and transport.
SIGNORiP04114.

Miscellaneous databases

ChiTaRSiAPOB. human.
GeneWikiiApolipoprotein_B.
GenomeRNAii338.
PROiP04114.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000084674.
ExpressionAtlasiP04114. baseline and differential.
GenevisibleiP04114. HS.

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]
SMARTiSM01169. DUF1943. 1 hit.
SM00638. LPD_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 2 hits.
PROSITEiPS51211. VITELLOGENIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 203 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.