CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002094
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Apolipoprotein B-100 
Protein Synonyms/Alias
 Apo B-100; Apolipoprotein B-48; Apo B-48 
Gene Name
 APOB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1778DNIYSSDKFYKQTVNacetylation[1]
2004DAYNTKDKIGVELTGacetylation[2]
2265IRIQIQEKLQQLKRHacetylation[1]
2911ADLRNEIKTLLKAGHubiquitination[3]
2915NEIKTLLKAGHIAWTubiquitination[3]
Reference
 [1] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 46 672 Vitellogenin.
 REGION 32 126 Heparin-binding.
 REGION 232 306 Heparin-binding.
 REGION 902 959 Heparin-binding.
 REGION 2043 2178 Heparin-binding.
 REGION 3161 3236 Heparin-binding.
 REGION 3174 3184 Basic (possible receptor binding region).
 REGION 3373 3393 LDL receptor binding.
 REGION 3383 3516 Heparin-binding.
 REGION 3386 3394 Basic (possible receptor binding region).
 MOD_RES 2004 2004 N6-acetyllysine.
 LIPID 1112 1112 S-palmitoyl cysteine.
 CARBOHYD 34 34 N-linked (GlcNAc...) (Potential).
 CARBOHYD 185 185 N-linked (GlcNAc...).
 CARBOHYD 983 983 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1368 1368 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1377 1377 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1523 1523 N-linked (GlcNAc...).
 CARBOHYD 2239 2239 N-linked (GlcNAc...).
 CARBOHYD 2560 2560 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2779 2779 N-linked (GlcNAc...).
 CARBOHYD 2982 2982 N-linked (GlcNAc...).
 CARBOHYD 3101 3101 N-linked (GlcNAc...).
 CARBOHYD 3224 3224 N-linked (GlcNAc...).
 CARBOHYD 3336 3336 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3358 3358 N-linked (GlcNAc...).
 CARBOHYD 3411 3411 N-linked (GlcNAc...).
 CARBOHYD 3465 3465 N-linked (GlcNAc...).
 CARBOHYD 3895 3895 N-linked (GlcNAc...).
 CARBOHYD 4237 4237 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4431 4431 N-linked (GlcNAc...) (Potential).
 DISULFID 39 88
 DISULFID 78 97
 DISULFID 186 212
 DISULFID 245 261
 DISULFID 385 390
 DISULFID 478 513
 DISULFID 966 976
 DISULFID 3194 3324  
Keyword
 Acetylation; Atherosclerosis; Cholesterol metabolism; Chylomicron; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Heparin-binding; LDL; Lipid metabolism; Lipid transport; Lipoprotein; Palmitate; Polymorphism; Reference proteome; RNA editing; Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport; VLDL. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 4563 AA 
Protein Sequence
MDPPRPALLA LLALPALLLL LLAGARAEEE MLENVSLVCP KDATRFKHLR KYTYNYEAES 60
SSGVPGTADS RSATRINCKV ELEVPQLCSF ILKTSQCTLK EVYGFNPEGK ALLKKTKNSE 120
EFAAAMSRYE LKLAIPEGKQ VFLYPEKDEP TYILNIKRGI ISALLVPPET EEAKQVLFLD 180
TVYGNCSTHF TVKTRKGNVA TEISTERDLG QCDRFKPIRT GISPLALIKG MTRPLSTLIS 240
SSQSCQYTLD AKRKHVAEAI CKEQHLFLPF SYKNKYGMVA QVTQTLKLED TPKINSRFFG 300
EGTKKMGLAF ESTKSTSPPK QAEAVLKTLQ ELKKLTISEQ NIQRANLFNK LVTELRGLSD 360
EAVTSLLPQL IEVSSPITLQ ALVQCGQPQC STHILQWLKR VHANPLLIDV VTYLVALIPE 420
PSAQQLREIF NMARDQRSRA TLYALSHAVN NYHKTNPTGT QELLDIANYL MEQIQDDCTG 480
DEDYTYLILR VIGNMGQTME QLTPELKSSI LKCVQSTKPS LMIQKAAIQA LRKMEPKDKD 540
QEVLLQTFLD DASPGDKRLA AYLMLMRSPS QADINKIVQI LPWEQNEQVK NFVASHIANI 600
LNSEELDIQD LKKLVKEALK ESQLPTVMDF RKFSRNYQLY KSVSLPSLDP ASAKIEGNLI 660
FDPNNYLPKE SMLKTTLTAF GFASADLIEI GLEGKGFEPT LEALFGKQGF FPDSVNKALY 720
WVNGQVPDGV SKVLVDHFGY TKDDKHEQDM VNGIMLSVEK LIKDLKSKEV PEARAYLRIL 780
GEELGFASLH DLQLLGKLLL MGARTLQGIP QMIGEVIRKG SKNDFFLHYI FMENAFELPT 840
GAGLQLQISS SGVIAPGAKA GVKLEVANMQ AELVAKPSVS VEFVTNMGII IPDFARSGVQ 900
MNTNFFHESG LEAHVALKAG KLKFIIPSPK RPVKLLSGGN TLHLVSTTKT EVIPPLIENR 960
QSWSVCKQVF PGLNYCTSGA YSNASSTDSA SYYPLTGDTR LELELRPTGE IEQYSVSATY 1020
ELQREDRALV DTLKFVTQAE GAKQTEATMT FKYNRQSMTL SSEVQIPDFD VDLGTILRVN 1080
DESTEGKTSY RLTLDIQNKK ITEVALMGHL SCDTKEERKI KGVISIPRLQ AEARSEILAH 1140
WSPAKLLLQM DSSATAYGST VSKRVAWHYD EEKIEFEWNT GTNVDTKKMT SNFPVDLSDY 1200
PKSLHMYANR LLDHRVPQTD MTFRHVGSKL IVAMSSWLQK ASGSLPYTQT LQDHLNSLKE 1260
FNLQNMGLPD FHIPENLFLK SDGRVKYTLN KNSLKIEIPL PFGGKSSRDL KMLETVRTPA 1320
LHFKSVGFHL PSREFQVPTF TIPKLYQLQV PLLGVLDLST NVYSNLYNWS ASYSGGNTST 1380
DHFSLRARYH MKADSVVDLL SYNVQGSGET TYDHKNTFTL SYDGSLRHKF LDSNIKFSHV 1440
EKLGNNPVSK GLLIFDASSS WGPQMSASVH LDSKKKQHLF VKEVKIDGQF RVSSFYAKGT 1500
YGLSCQRDPN TGRLNGESNL RFNSSYLQGT NQITGRYEDG TLSLTSTSDL QSGIIKNTAS 1560
LKYENYELTL KSDTNGKYKN FATSNKMDMT FSKQNALLRS EYQADYESLR FFSLLSGSLN 1620
SHGLELNADI LGTDKINSGA HKATLRIGQD GISTSATTNL KCSLLVLENE LNAELGLSGA 1680
SMKLTTNGRF REHNAKFSLD GKAALTELSL GSAYQAMILG VDSKNIFNFK VSQEGLKLSN 1740
DMMGSYAEMK FDHTNSLNIA GLSLDFSSKL DNIYSSDKFY KQTVNLQLQP YSLVTTLNSD 1800
LKYNALDLTN NGKLRLEPLK LHVAGNLKGA YQNNEIKHIY AISSAALSAS YKADTVAKVQ 1860
GVEFSHRLNT DIAGLASAID MSTNYNSDSL HFSNVFRSVM APFTMTIDAH TNGNGKLALW 1920
GEHTGQLYSK FLLKAEPLAF TFSHDYKGST SHHLVSRKSI SAALEHKVSA LLTPAEQTGT 1980
WKLKTQFNNN EYSQDLDAYN TKDKIGVELT GRTLADLTLL DSPIKVPLLL SEPINIIDAL 2040
EMRDAVEKPQ EFTIVAFVKY DKNQDVHSIN LPFFETLQEY FERNRQTIIV VLENVQRNLK 2100
HINIDQFVRK YRAALGKLPQ QANDYLNSFN WERQVSHAKE KLTALTKKYR ITENDIQIAL 2160
DDAKINFNEK LSQLQTYMIQ FDQYIKDSYD LHDLKIAIAN IIDEIIEKLK SLDEHYHIRV 2220
NLVKTIHDLH LFIENIDFNK SGSSTASWIQ NVDTKYQIRI QIQEKLQQLK RHIQNIDIQH 2280
LAGKLKQHIE AIDVRVLLDQ LGTTISFERI NDILEHVKHF VINLIGDFEV AEKINAFRAK 2340
VHELIERYEV DQQIQVLMDK LVELAHQYKL KETIQKLSNV LQQVKIKDYF EKLVGFIDDA 2400
VKKLNELSFK TFIEDVNKFL DMLIKKLKSF DYHQFVDETN DKIREVTQRL NGEIQALELP 2460
QKAEALKLFL EETKATVAVY LESLQDTKIT LIINWLQEAL SSASLAHMKA KFRETLEDTR 2520
DRMYQMDIQQ ELQRYLSLVG QVYSTLVTYI SDWWTLAAKN LTDFAEQYSI QDWAKRMKAL 2580
VEQGFTVPEI KTILGTMPAF EVSLQALQKA TFQTPDFIVP LTDLRIPSVQ INFKDLKNIK 2640
IPSRFSTPEF TILNTFHIPS FTIDFVEMKV KIIRTIDQML NSELQWPVPD IYLRDLKVED 2700
IPLARITLPD FRLPEIAIPE FIIPTLNLND FQVPDLHIPE FQLPHISHTI EVPTFGKLYS 2760
ILKIQSPLFT LDANADIGNG TTSANEAGIA ASITAKGESK LEVLNFDFQA NAQLSNPKIN 2820
PLALKESVKF SSKYLRTEHG SEMLFFGNAI EGKSNTVASL HTEKNTLELS NGVIVKINNQ 2880
LTLDSNTKYF HKLNIPKLDF SSQADLRNEI KTLLKAGHIA WTSSGKGSWK WACPRFSDEG 2940
THESQISFTI EGPLTSFGLS NKINSKHLRV NQNLVYESGS LNFSKLEIQS QVDSQHVGHS 3000
VLTAKGMALF GEGKAEFTGR HDAHLNGKVI GTLKNSLFFS AQPFEITAST NNEGNLKVRF 3060
PLRLTGKIDF LNNYALFLSP SAQQASWQVS ARFNQYKYNQ NFSAGNNENI MEAHVGINGE 3120
ANLDFLNIPL TIPEMRLPYT IITTPPLKDF SLWEKTGLKE FLKTTKQSFD LSVKAQYKKN 3180
KHRHSITNPL AVLCEFISQS IKSFDRHFEK NRNNALDFVT KSYNETKIKF DKYKAEKSHD 3240
ELPRTFQIPG YTVPVVNVEV SPFTIEMSAF GYVFPKAVSM PSFSILGSDV RVPSYTLILP 3300
SLELPVLHVP RNLKLSLPDF KELCTISHIF IPAMGNITYD FSFKSSVITL NTNAELFNQS 3360
DIVAHLLSSS SSVIDALQYK LEGTTRLTRK RGLKLATALS LSNKFVEGSH NSTVSLTTKN 3420
MEVSVATTTK AQIPILRMNF KQELNGNTKS KPTVSSSMEF KYDFNSSMLY STAKGAVDHK 3480
LSLESLTSYF SIESSTKGDV KGSVLSREYS GTIASEANTY LNSKSTRSSV KLQGTSKIDD 3540
IWNLEVKENF AGEATLQRIY SLWEHSTKNH LQLEGLFFTN GEHTSKATLE LSPWQMSALV 3600
QVHASQPSSF HDFPDLGQEV ALNANTKNQK IRWKNEVRIH SGSFQSQVEL SNDQEKAHLD 3660
IAGSLEGHLR FLKNIILPVY DKSLWDFLKL DVTTSIGRRQ HLRVSTAFVY TKNPNGYSFS 3720
IPVKVLADKF IIPGLKLNDL NSVLVMPTFH VPFTDLQVPS CKLDFREIQI YKKLRTSSFA 3780
LNLPTLPEVK FPEVDVLTKY SQPEDSLIPF FEITVPESQL TVSQFTLPKS VSDGIAALDL 3840
NAVANKIADF ELPTIIVPEQ TIEIPSIKFS VPAGIVIPSF QALTARFEVD SPVYNATWSA 3900
SLKNKADYVE TVLDSTCSST VQFLEYELNV LGTHKIEDGT LASKTKGTFA HRDFSAEYEE 3960
DGKYEGLQEW EGKAHLNIKS PAFTDLHLRY QKDKKGISTS AASPAVGTVG MDMDEDDDFS 4020
KWNFYYSPQS SPDKKLTIFK TELRVRESDE ETQIKVNWEE EAASGLLTSL KDNVPKATGV 4080
LYDYVNKYHW EHTGLTLREV SSKLRRNLQN NAEWVYQGAI RQIDDIDVRF QKAASGTTGT 4140
YQEWKDKAQN LYQELLTQEG QASFQGLKDN VFDGLVRVTQ EFHMKVKHLI DSLIDFLNFP 4200
RFQFPGKPGI YTREELCTMF IREVGTVLSQ VYSKVHNGSE ILFSYFQDLV ITLPFELRKH 4260
KLIDVISMYR ELLKDLSKEA QEVFKAIQSL KTTEVLRNLQ DLLQFIFQLI EDNIKQLKEM 4320
KFTYLINYIQ DEINTIFSDY IPYVFKLLKE NLCLNLHKFN EFIQNELQEA SQELQQIHQY 4380
IMALREEYFD PSIVGWTVKY YELEEKIVSL IKNLLVALKD FHSEYIVSAS NFTSQLSSQV 4440
EQFLHRNIQE YLSILTDPDG KGKEKIAELS ATAQEIIKSQ AIATKKIISD YHQQFRYKLQ 4500
DFSDQLSDYY EKFIAESKRL IDLSIQNYHT FLIYITELLK KLQSTTVMNP YMKLAPGELT 4560
IIL 4563 
Gene Ontology
 GO:0034360; C:chylomicron remnant; TAS:BHF-UCL.
 GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005769; C:early endosome; TAS:Reactome.
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0031904; C:endosome lumen; TAS:Reactome.
 GO:0010008; C:endosome membrane; TAS:Reactome.
 GO:0034363; C:intermediate-density lipoprotein particle; IDA:BHF-UCL.
 GO:0034362; C:low-density lipoprotein particle; IDA:BHF-UCL.
 GO:0034359; C:mature chylomicron; IDA:BHF-UCL.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
 GO:0031983; C:vesicle lumen; IEA:Compara.
 GO:0017127; F:cholesterol transporter activity; IMP:BHF-UCL.
 GO:0008201; F:heparin binding; IDA:BHF-UCL.
 GO:0050750; F:low-density lipoprotein particle receptor binding; IMP:BHF-UCL.
 GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
 GO:0048844; P:artery morphogenesis; IEA:Compara.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0071379; P:cellular response to prostaglandin stimulus; IEA:Compara.
 GO:0071356; P:cellular response to tumor necrosis factor; IEA:Compara.
 GO:0033344; P:cholesterol efflux; IEA:Compara.
 GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
 GO:0008203; P:cholesterol metabolic process; IMP:BHF-UCL.
 GO:0009566; P:fertilization; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO:0042158; P:lipoprotein biosynthetic process; IEA:Compara.
 GO:0042159; P:lipoprotein catabolic process; IEA:Compara.
 GO:0042157; P:lipoprotein metabolic process; TAS:Reactome.
 GO:0042953; P:lipoprotein transport; IEA:Compara.
 GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
 GO:0034374; P:low-density lipoprotein particle remodeling; IMP:BHF-UCL.
 GO:0007399; P:nervous system development; IEA:Compara.
 GO:0007603; P:phototransduction, visible light; TAS:Reactome.
 GO:0010886; P:positive regulation of cholesterol storage; IDA:BHF-UCL.
 GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
 GO:0009791; P:post-embryonic development; IEA:Compara.
 GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
 GO:0045540; P:regulation of cholesterol biosynthetic process; IEA:Compara.
 GO:0009743; P:response to carbohydrate stimulus; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
 GO:0010269; P:response to selenium ion; IEA:Compara.
 GO:0009615; P:response to virus; IEP:UniProtKB.
 GO:0001523; P:retinoid metabolic process; TAS:Reactome.
 GO:0030317; P:sperm motility; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0019433; P:triglyceride catabolic process; IEA:Compara.
 GO:0006642; P:triglyceride mobilization; IEA:Compara.
 GO:0034379; P:very-low-density lipoprotein particle assembly; IC:BHF-UCL. 
Interpro
 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. 
Pfam
 PF12491; ApoB100_C
 PF06448; DUF1081
 PF09172; DUF1943
 PF01347; Vitellogenin_N 
SMART
 SM00638; LPD_N 
PROSITE
 PS51211; VITELLOGENIN 
PRINTS