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E9Q414

- APOB_MOUSE

UniProt

E9Q414 - APOB_MOUSE

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Protein

Apolipoprotein B-100

Gene
Apob
Organism
Mus musculus (Mouse)
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: Ensembl
  2. heparin binding Source: UniProtKB-KW
  3. phospholipid binding Source: Ensembl

GO - Biological processi

  1. artery morphogenesis Source: MGI
  2. cellular response to prostaglandin stimulus Source: Ensembl
  3. cellular response to tumor necrosis factor Source: Ensembl
  4. cholesterol efflux Source: MGI
  5. cholesterol homeostasis Source: MGI
  6. cholesterol metabolic process Source: UniProtKB-KW
  7. cholesterol transport Source: MGI
  8. fertilization Source: MGI
  9. in utero embryonic development Source: MGI
  10. lipid catabolic process Source: MGI
  11. lipid metabolic process Source: MGI
  12. lipoprotein biosynthetic process Source: MGI
  13. lipoprotein catabolic process Source: MGI
  14. lipoprotein metabolic process Source: MGI
  15. lipoprotein transport Source: MGI
  16. low-density lipoprotein particle clearance Source: Ensembl
  17. low-density lipoprotein particle remodeling Source: Ensembl
  18. nervous system development Source: MGI
  19. positive regulation of cholesterol storage Source: Ensembl
  20. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
  21. post-embryonic development Source: MGI
  22. regulation of cholesterol biosynthetic process Source: MGI
  23. response to carbohydrate Source: Ensembl
  24. response to lipopolysaccharide Source: Ensembl
  25. response to selenium ion Source: Ensembl
  26. response to virus Source: Ensembl
  27. spermatogenesis Source: MGI
  28. sperm motility Source: MGI
  29. triglyceride catabolic process Source: MGI
  30. triglyceride mobilization Source: MGI
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_196581. Scavenging by Class A Receptors.
REACT_196592. Scavenging by Class B Receptors.
REACT_196594. Scavenging by Class H Receptors.
REACT_196603. Scavenging by Class F Receptors.
REACT_198569. Retinoid metabolism and transport.
REACT_216017. Chylomicron-mediated lipid transport.
REACT_222614. LDL-mediated lipid transport.
REACT_225233. Cell surface interactions at the vascular wall.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:88052. Apob.

Subcellular locationi

Cytoplasm By similarity. Secreted By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. extracellular region Source: Reactome
  3. intermediate-density lipoprotein particle Source: Ensembl
  4. low-density lipoprotein particle Source: UniProtKB-KW
  5. mature chylomicron Source: Ensembl
  6. very-low-density lipoprotein particle Source: UniProtKB-KW
  7. vesicle lumen Source: Ensembl
  8. vesicle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chylomicron, Cytoplasm, LDL, Secreted, VLDL

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 Reviewed predictionAdd
BLAST
Chaini28 – 45054478Apolipoprotein B-100PRO_0000420969Add
BLAST
Chaini28 – 21782151Apolipoprotein B-48PRO_0000420970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi39 ↔ 88 By similarity
Disulfide bondi78 ↔ 97 By similarity
Glycosylationi185 – 1851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi186 ↔ 212 By similarity
Disulfide bondi245 ↔ 261 By similarity
Disulfide bondi385 ↔ 390 By similarity
Disulfide bondi478 ↔ 513 By similarity
Disulfide bondi966 ↔ 976 By similarity
Glycosylationi983 – 9831N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1368 – 13681N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1377 – 13771N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1523 – 15231N-linked (GlcNAc...) Reviewed prediction
Modified residuei2005 – 20051N6-acetyllysine By similarity
Glycosylationi2554 – 25541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2773 – 27731N-linked (GlcNAc...)1 Publication
Glycosylationi2976 – 29761N-linked (GlcNAc...)1 Publication
Glycosylationi3095 – 30951N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3331 – 33311N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3353 – 33531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3460 – 34601N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3860 – 38601N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle By similarity.

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

MaxQBiE9Q414.
PRIDEiE9Q414.

Expressioni

Gene expression databases

BgeeiE9Q414.

Interactioni

Subunit structurei

Interacts with PCSK9 By similarity.

Protein-protein interaction databases

IntActiE9Q414. 3 interactions.
MINTiMINT-1846293.
STRINGi10090.ENSMUSP00000035761.

Structurei

3D structure databases

ProteinModelPortaliE9Q414.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 12695Heparin-binding By similarityAdd
BLAST
Regioni232 – 30675Heparin-binding By similarityAdd
BLAST
Regioni902 – 95958Heparin-binding By similarityAdd
BLAST
Regioni2042 – 2177136Heparin-binding By similarityAdd
BLAST
Regioni3155 – 323076Heparin-binding By similarityAdd
BLAST
Regioni3168 – 317811Basic (possible receptor binding region) By similarityAdd
BLAST
Regioni3368 – 338821LDL receptor binding By similarityAdd
BLAST
Regioni3378 – 3511134Heparin-binding By similarityAdd
BLAST
Regioni3381 – 33899Basic (possible receptor binding region) By similarity

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat, Signal

Phylogenomic databases

GeneTreeiENSGT00590000083139.
KOiK14462.
OMAiHIPEFQL.
OrthoDBiEOG7VB2DG.
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.
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]
SUPFAMiSSF48431. 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.

E9Q414-1 [UniParc]FASTAAdd to Basket

« Hide

MGPRKPALRT PLLLLFLLLF LDTSVWAQDE VLENLSFSCP KDATRFKHLR     50
KYVYNYEAES SSGVQGTADS RSATKINCKV ELEVPQICGF IMRTNQCTLK 100
EVYGFNPEGK ALMKKTKNSE EFAAAMSRYE LKLAIPEGKQ IVLYPDKDEP 150
KYILNIKRGI ISALLVPPET EEDQQELFLD TVYGNCSTQV TVNSRKGTVP 200
TEMSTERNLQ QCDGFQPIST SVSPLALIKG LVHPLSTLIS SSQTCQYTLD 250
PKRKHVSEAV CDEQHLFLPF SYKNKYGIMT RVTQKLSLED TPKINSRFFS 300
EGTNRMGLAF ESTKSTSSPK QADAVLKTLQ ELKKLSISEQ NAQRANLFNK 350
LVTELRGLTG EAITSLLPQL IEVSSPITLQ ALVQCGQPQC YTHILQWLKT 400
EKAHPLLVDI VTYLMALIPN PSTQRLQEIF NTAKEQQSRA TLYALSHAVN 450
SYFDVDHSRS PVLQDIAGYL LKQIDNECTG NEDHTFLILR VIGNMGRTME 500
QVMPALKSSV LSCVRSTKPS LLIQKAALQA LRKMELEDEV RTILFDTFVN 550
GVAPVEKRLA AYLLLMKNPS SSDINKIAQL LQWEQSEQVK NFVASHIANI 600
LNSEELYVQD LKVLIKNALE NSQFPTIMDF RKFSRNYQIS KSASLPMFDP 650
VSVKIEGNLI FDPSSYLPRE SLLKTTLTVF GLASLDLFEI GLEGKGFEPT 700
LEALFGKQGF FPDSVNKALY WVNGRVPDGV SKVLVDHFGY TTDGKHEQDM 750
VNGIMPIVDK LIKDLKSKEI PEARAYLRIL GKELSFVRLQ DLQVLGKLLL 800
SGAQTLQGIP QMVVQAIREG SKNDLFLHYI FMDNAFELPT GAGLQLQVSS 850
SGVFTPGIKA GVRLELANIQ AELVAKPSVS LEFVTNMGII IPDFAKSSVQ 900
MNTNFFHESG LEARVALKAG QLKVIIPSPK RPVKLFSGSN TLHLVSTTKT 950
EVIPPLVENR QSWSTCKPLF TGMNYCTTGA YSNASSTESA SYYPLTGDTR 1000
YELELRPTGE VEQYSATATY ELLKEDKSLV DTLKFLVQAE GVQQSEATVL 1050
FKYNRRSRTL SSEVLIPGFD VNFGTILRVN DESAKDKNTY KLILDIQNKK 1100
ITEVSLVGHL SYDKKGDGKI KGVVSIPRLQ AEARSEVHTH WSSTKLLFQM 1150
DSSATAYGST ISKRVTWRYD NEIIEFDWNT GTNVDTKKVA SNFPVDLSHY 1200
PRMLHEYANG LLDHRVPQTD VTFRDMGSKL IVATNTWLQM ATRGLPYPQT 1250
LQDHLNSLSE LNLLKMGLSD FHIPDNLFLK TDGRVKYTMN RNKINIDIPL 1300
PLGGKSSKDL KMPESVRTPA LNFKSVGFHL PSREVQVPTF TIPKTHQLQV 1350
PLLGVLDLST NVYSNLYNWS ASYTGGNTSR DHFSLQAQYR MKTDSVVDLF 1400
SYSVQGSGET TYDSKNTFTL SCDGSLHHKF LDSKFKVSHV EKFGNSPVSK 1450
GLLTFETSSA LGPQMSATVH LDSKKKQHLY VKDIKVDGQF RASSFYAQGK 1500
YGLSCERDVT TGQLSGESNM RFNSTYFQGT NQIVGMYQDG ALSITSTSDL 1550
QDGIFKNTAS LKYENYELTL KSDSSGQYEN FAASNKLDVT FSTQSALLRS 1600
EHQANYKSLR LVTLLSGSLT SQGVELNADI LGTDKINTGA HKATLKIARD 1650
GLSTSATTNL KYSPLLLENE LNAELGLSGA SMKLSTNGRF KEHHAKFSLD 1700
GRAALTEVSL GSIYQAMILG ADSKNIFNFK LSREGLRLSN DLMGSYAEMK 1750
LDHTHSLNIA GLSLDFFSKM DNIYSGDKFY KQNFNLQLQP YSFITTLSND 1800
LRYGALDLTN NGRFRLEPLK LNVGGNFKGT YQNNELKHIY TISYTDLVVA 1850
SYRADTVAKV QGVEFSHRLN ADIEGLTSSV DVTTSYNSDP LHFNNVFHFS 1900
LAPFTLGIDT HTSGDGKLSF WGEHTGQLYS KFLLKAEPLA LIVSHDYKGS 1950
TSHSLPYESS ISTALEHTVS ALLTPAEQTS TWKFKTKLND KVYSQDFEAY 2000
NTKDKIGVEL SGRADLSGLY SPIKLPFFYS EPVNVLNGLE VNDAVDKPQE 2050
FTIIAVVKYD KNQDVHTINL PFFKSLPDYL ERNRRGMISL LEAMRGELQR 2100
LSVDQFVRKY RAALSRLPQQ IHHYLNASDW ERQVAGAKEK ITSFMENYRI 2150
TDNDVLIAID SAKINFNEKL SQLETYAIQF DQYIKDNYDP HDLKRTIAEI 2200
IDRIIEKLKI LDEQYHIRVN LAKSIHNLYL FVENVDLNQV SSSNTSWIQN 2250
VDSNYQVRIQ IQEKLQQLRT QIQNIDIQQL AAEVKRQMDA IDVTMHLDQL 2300
RTAILFQRIS DIIDRVKYFV MNLIEDFKVT EKINTFRVIV RELIEKYEVD 2350
QHIQVLMDKS VELAHRYSLS EPLQKLSNVL QRIEIKDYYE KLVGFIDDTV 2400
EWLKALSFKN TIEELNRLTD MLVKKLKAFD YHQFVDKTNS KIREMTQRIN 2450
AEIQALKLPQ KMEALKLLVE DFKTTVSNSL ERLKDTKVTV VIDWLQDILT 2500
QMKDHFQDTL EDVRDRIYQM DIQRELEHFL SLVNQVYSTL VTYMSDWWTL 2550
TAKNITDFAE QYSIQNWAES IKVLVEQGFI VPEMQTFLWT MPAFEVSLRA 2600
LQEGNFQTPV FIVPLTDLRI PSIRINFKML KNIKIPLRFS TPEFTLLNTF 2650
HVHSFTIDLL EIKAKIIRTI DQILSSELQW PLPEMYLRDL DVVNIPLARL 2700
TLPDFHVPEI TIPEFTIPNV NLKDLHVPDL HIPEFQLPHL SHTIEIPAFG 2750
KLHSILKIQS PLFILDANAN IQNVTTSGNK AEIVASVTAK GESQFEALNF 2800
DFQAQAQFLE LNPHPPVLKE SMNFSSKHVR MEHEGEIVFD GKAIEGKSDT 2850
VASLHTEKNE VEFNNGMTVK VNNQLTLDSH TKYFHKLSVP RLDFSSKASL 2900
NNEIKTLLEA GHVALTSSGT GSWNWACPNF SDEGIHSSQI SFTVDGPIAF 2950
VGLSNNINGK HLRVIQKLTY ESGFLNYSKF EVESKVESQH VGSSILTANG 3000
RALLKDAKAE MTGEHNANLN GKVIGTLKNS LFFSAQPFEI TASTNNEGNL 3050
KVGFPLKLTG KIDFLNNYAL FLSPRAQQAS WQASTRFNQY KYNQNFSAIN 3100
NEHNIEASIG MNGDANLDFL NIPLTIPEIN LPYTEFKTPL LKDFSIWEET 3150
GLKEFLKTTK QSFDLSVKAQ YKKNSDKHSI VVPLGMFYEF ILNNVNSWDR 3200
KFEKVRNNAL HFLTTSYNEA KIKVDKYKTE NSLNQPSGTF QNHGYTIPVV 3250
NIEVSPFAVE TLASSHVIPT AISTPSVTIP GPNIMVPSYK LVLPPLELPV 3300
FHGPGNLFKF FLPDFKGFNT IDNIYIPAMG NFTYDFSFKS SVITLNTNAG 3350
LYNQSDIVAH FLSSSSFVTD ALQYKLEGTS RLMRKRGLKL ATAVSLTNKF 3400
VKGSHDSTIS LTKKNMEASV RTTANLHAPI FSMNFKQELN GNTKSKPTVS 3450
SSIELNYDFN SSKLHSTATG GIDHKFSLES LTSYFSIESF TKGNIKSSFL 3500
SQEYSGSVAN EANVYLNSKG TRSSVRLQGA SKVDGIWNVE VGENFAGEAT 3550
LQRIYTTWEH NMKNHLQVYS YFFTKGKQTC RATLELSPWT MSTLLQVHVS 3600
QLSSLLDLHH FDQEVILKAN TKNQKISWKG GVQVESRVLQ HNAQFSNDQE 3650
EIRLDLAGSL DGQLWDLEAI FLPVYGKSLQ ELLQMDGKRQ YLQASTSLLY 3700
TKNPNGYLLS LPVQELADRF IIPGIKLNDF SGVKIYKKLS TSPFALNLTM 3750
LPKVKFPGID LLTQYSTPEG SSVPIFEATI PEIHLTVSQF TLPKSLPVGN 3800
TVFDLNKLAN MIADVDLPSV TLPEQTIVIP PLEFSVPAGI FIPFFGELTA 3850
RAGMASPLYN VTWSAGWKTK ADHVETFLDS MCTSTLQFLE YALKVVETHK 3900
IEEDLLTYNI KGTLQHCDFN VEYNEDGLFK GLWDWQGEAH LDITSPALTD 3950
FHLYYKEDKT SLSASAASST IGTVGLDSST DDQSVELNVY FHPQSPPEKK 4000
LSIFKTEWRY KESDGERYIK INWEEEAASR LLGSLKSNVP KASKAIYDYA 4050
NKYHLEYVSS ELRKSLQVNA EHARRMVDEM NMSFQRVARD TYQNLYEEML 4100
AQKSLSIPEN LKKRVLDSIV HVTQKYHMAV MWLMDSFIHF LKFNRVQFPG 4150
YAGTYTVDEL YTIVMKETKK SLSQLFNGLG NLLSYVQNQV EKSRLINDIT 4200
FKCPFFSKPC KLKDLILIFR EELNILSNIG QQDIKFTTIL SSLQGFLERV 4250
LDIIEEQIKC LKDNESTCVA DHINMVFKIQ VPYAFKSLRE DIYFVLGEFN 4300
DFLQSILQEG SYKLQQVHQY MKALREEYFD PSMVGWTVKY YEIEENMVEL 4350
IKTLLVSFRD VYSEYSVTAA DFASKMSTQV EQFVSRDIRE YLSMLTDING 4400
KWMEKIAELS IVAKETMKSW VTAVAKIMSD YPQQFHSNLQ DFSDQLSSYY 4450
EKFVGESTRL IDLSIQNYHV FLRYITELLR KLQVATANNV SPYIKLAQGE 4500
LMITF 4505
Length:4,505
Mass (Da):509,432
Last modified:April 5, 2011 - v1
Checksum:i09EADB2D499E7A82
GO

Sequence cautioni

The sequence AAI41358.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAI41361.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAE27983.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

RNA editingi

The stop codon (UAA) at position 2179 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 By similarity.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 422KD → N in AAI00608. 1 Publication
Sequence conflicti331 – 3322EL → KK in AAI00608. 1 Publication
Sequence conflicti335 – 3351L → K in AAI00608. 1 Publication
Sequence conflicti1477 – 14771Q → K in AAH38263. 1 Publication
Sequence conflicti3265 – 32651S → R in AAA37246. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC163900 Genomic DNA. No translation available.
BC038263 mRNA. Translation: AAH38263.1.
BC100607 mRNA. Translation: AAI00608.1.
BC141357 mRNA. Translation: AAI41358.1. Different initiation.
BC141360 mRNA. Translation: AAI41361.1. Different initiation.
M35186 Genomic DNA. Translation: AAA37246.1.
X15191 Genomic DNA. Translation: CAA33265.1.
AK147540 mRNA. Translation: BAE27983.1. Different initiation.
CCDSiCCDS49022.1.
RefSeqiNP_033823.2. NM_009693.2.
UniGeneiMm.221239.

Genome annotation databases

EnsembliENSMUST00000037811; ENSMUSP00000036044; ENSMUSG00000020609.
GeneIDi238055.
KEGGimmu:238055.
UCSCiuc007mzf.2. mouse.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC163900 Genomic DNA. No translation available.
BC038263 mRNA. Translation: AAH38263.1 .
BC100607 mRNA. Translation: AAI00608.1 .
BC141357 mRNA. Translation: AAI41358.1 . Different initiation.
BC141360 mRNA. Translation: AAI41361.1 . Different initiation.
M35186 Genomic DNA. Translation: AAA37246.1 .
X15191 Genomic DNA. Translation: CAA33265.1 .
AK147540 mRNA. Translation: BAE27983.1 . Different initiation.
CCDSi CCDS49022.1.
RefSeqi NP_033823.2. NM_009693.2.
UniGenei Mm.221239.

3D structure databases

ProteinModelPortali E9Q414.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi E9Q414. 3 interactions.
MINTi MINT-1846293.
STRINGi 10090.ENSMUSP00000035761.

Proteomic databases

MaxQBi E9Q414.
PRIDEi E9Q414.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000037811 ; ENSMUSP00000036044 ; ENSMUSG00000020609 .
GeneIDi 238055.
KEGGi mmu:238055.
UCSCi uc007mzf.2. mouse.

Organism-specific databases

CTDi 338.
MGIi MGI:88052. Apob.

Phylogenomic databases

GeneTreei ENSGT00590000083139.
KOi K14462.
OMAi HIPEFQL.
OrthoDBi EOG7VB2DG.
TreeFami TF331316.

Enzyme and pathway databases

Reactomei REACT_196581. Scavenging by Class A Receptors.
REACT_196592. Scavenging by Class B Receptors.
REACT_196594. Scavenging by Class H Receptors.
REACT_196603. Scavenging by Class F Receptors.
REACT_198569. Retinoid metabolism and transport.
REACT_216017. Chylomicron-mediated lipid transport.
REACT_222614. LDL-mediated lipid transport.
REACT_225233. Cell surface interactions at the vascular wall.

Miscellaneous databases

ChiTaRSi APOB. mouse.
NextBioi 383653.
PROi E9Q414.
SOURCEi Search...

Gene expression databases

Bgeei E9Q414.

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.
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 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 [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1477 AND 3004-4505.
    Strain: FVB/N.
    Tissue: Liver.
  3. "Sequence of the putative low-density lipoprotein receptor-binding regions of apolipoprotein B in mouse and hamster."
    Smith T.J., Hautamaa D., Maeda N.
    Gene 87:309-310(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2734-3518.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2962-4505.
    Strain: C57BL/6J.
    Tissue: Placenta.
  5. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2773 AND ASN-2976.
    Strain: C57BL/6.
    Tissue: Plasma.

Entry informationi

Entry nameiAPOB_MOUSE
AccessioniPrimary (citable) accession number: E9Q414
Secondary accession number(s): Q3UH74
, Q497D8, Q61314, Q61318, Q8CGG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2013
Last sequence update: April 5, 2011
Last modified: September 3, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3