Target Information
| Target General Information | Top | |||||
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| Target ID |
T00494
(Former ID: TTDR00288)
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| Target Name |
ATP-binding cassette transporter A1 (ABCA1)
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| Synonyms |
Cholesterol mobilizing transporter ABCA1; Cholesterol efflux regulatory protein; CERP; ATP-binding cassette transporter (ABCA1) transmembrane protein; ATP-binding cassette sub-family A member 1; ATP-binding cassette 1; ABC1; ABC-1
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| Gene Name |
ABCA1
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| Target Type |
Successful target
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[1] | ||||
| Disease | [+] 1 Target-related Diseases | + | ||||
| 1 | Coronary atherosclerosis [ICD-11: BA80] | |||||
| Function |
Involved in the efflux of intracellular cholesterol and phospholipids and their transfer to apoliproteins to form nascent high density lipoproteins/HDLs. cAMP-dependent and sulfonylurea-sensitive anion transporter.
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| BioChemical Class |
ABC transporter
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| UniProt ID | ||||||
| EC Number |
EC 7.6.2.1
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| Sequence |
MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKA
MPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDT SMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILH KVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPIL RTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQI YQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMK NLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELS PKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGS VYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTG ITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVV EQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIV YEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFV FLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFAS LLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTW YIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVS IQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIL GKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVG LPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLS SCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDI GHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAE TSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVK GWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQ PWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAP VPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDL TGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKK HLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQK GENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQER VSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLAL LLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNIN DILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEG VVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKI YRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSN IHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEK YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLT SHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFG LAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNF AKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV Click to Show/Hide
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| 3D Structure | Click to Show 3D Structure of This Target | PDB | ||||
| HIT2.0 ID | T61DYZ | |||||
| Drugs and Modes of Action | Top | |||||
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| Approved Drug(s) | [+] 1 Approved Drugs | + | ||||
| 1 | Probucol | Drug Info | Approved | Coronary artery disease | [2], [3] | |
| Discontinued Drug(s) | [+] 1 Discontinued Drugs | + | ||||
| 1 | RG-7273 | Drug Info | Discontinued in Phase 1 | Lipid metabolism disorder | [4] | |
| Mode of Action | [+] 2 Modes of Action | + | ||||
| Modulator | [+] 2 Modulator drugs | + | ||||
| 1 | Probucol | Drug Info | [1] | |||
| 2 | RG7232 | Drug Info | [6] | |||
| Inducer | [+] 1 Inducer drugs | + | ||||
| 1 | RG-7273 | Drug Info | [5] | |||
| Cell-based Target Expression Variations | Top | |||||
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| Cell-based Target Expression Variations | ||||||
| Drug Binding Sites of Target | Top | |||||
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| Ligand Name: Adenosine triphosphate | Ligand Info | |||||
| Structure Description | The structure of ATP-bound ABCA1 | PDB:7TBW | ||||
| Method | Electron microscopy | Resolution | 3.10 Å | Mutation | Yes | [7] |
| PDB Sequence |
CWPQLRLLLW
12 KNLTFRRRQT22 CQLLLEVAWP32 LFIFLILISV42 RLSYPPYEQH52 ECHFPNKAMP 62 SAGTLPWVQG72 IICNANNPCF82 RYPTPGEAPG92 VVGNFNKSIV102 ARLFSDARRL 112 LLYSQKDTSM122 KDMRKVLRTL132 QQIKKSSSKS200 EEMIQLGDQE210 VSELCGLPRE 220 KLAAAERVLR230 SNMDILKPIL240 RTLNSTSPFP250 SKELAEATKT260 LLHSLGTLAQ 270 ELFSMRSWSD280 MRQEVMFLTS296 STQIYQAVSR306 IVCGHTPYCN356 DLMKNLESSP 366 LSRIIWKALK376 PLLVGKILYT386 PDTPATRQVM396 AEVNKTFQEL406 AVFHDLEGMW 416 EELSPKIWTF426 MENSQEMDLV436 RMLLDSRDND446 HFWEQQLDGL456 DWTAQDIVAF 466 LAKHPVYTWR485 EAFNETNQAI495 RTISRFMECV505 NLNKLEPIAT515 EVWLINKSME 525 LLDERKFWAG535 IVFTGITPGS545 IELPHHVKYK555 IRMDIDNVER565 TNKIKDGYWD 575 PGPRADPFED585 MRYVWGGFAY595 LQDVVEQAII605 RVLTGTEKKT615 GVYMQQMPYP 625 CYVDDIFLRV635 MSRSMPLFMT645 LAWIYSVAVI655 IKGIVYEKEA665 RLKETMRIMG 675 LDNSILWFSW685 FISSLIPLLV695 SAGLLVVILK705 LGNLLPYSDP715 SVVFVFLSVF 725 AVVTILQCFL735 ISTLFSRANL745 AAACGGIIYF755 TLYLPYVLCV765 AWRDYVGFTL 775 KIFASLLSPV785 AFGFGCEYFA795 LFEEQGIGVQ805 WDNLFESPVE815 EDGFNLTTSV 825 SMMLFDTFLY835 GVMTWYIEAV845 FPGQYGIPRP855 WYFPCEPTHL895 KLGVSIQNLV 905 KVYRDGMKVA915 VDGLALNFYE925 GQITSFLGHN935 GAGKTTTMSI945 LTGLFPPTSG 955 TAYILGKDIR965 SEMSTIRQNL975 GVCPQHNVLF985 DMLTVEEHIW995 FYARLKGLSE 1005 KHVKAEMEQM1015 ALDVGLPSSK1025 LKSKTSQLSG1035 GMQRKLSVAL1045 AFVGGSKVVI 1055 LDQPTAGVDP1065 YSRRGIWELL1075 LKYRQGRTII1085 LSTHHMDEAD1095 VLGDRIAIIS 1105 HGKLCCVGSS1115 LFLKNQLGTG1125 YYLTLVKSAI1183 SNLIRKHVSE1193 ARLVEDIGHE 1203 LTYVLPAFVE1220 LFHEIDDRIS1235 SYGISETTLE1245 EIFLKVAEES1255 GKGSYQVKGW 1322 KLTQQQFVAL1332 LWKRLLIARR1342 SRKGFFAQIV1352 LPAVFVCIAL1362 VFSLIVPPFG 1372 KYPSLELQPW1382 MYNEQYTFVS1392 NDAPEDTGTL1402 ELLNALTKDP1412 GFGTRCMEGN 1422 PIPDTPCQAG1432 EEEWTTAPVP1442 QTIMDLFQNG1452 NWTMQNPSPA1462 CQCSKMLPVC 1477 PPGAGGLPPP1487 QRKQNTADIL1497 QDLTGRNISD1507 YLVKTYVQII1517 AKSLKNKIWV 1527 NEFRYGGFSL1537 GVSNPSQEVN1552 DAIKQMKKHL1562 KLAKDSSADR1572 FLNSLGRFMT 1582 GLDTKNNVKV1592 WFNNKGWHAI1602 SSFLNVINNA1612 ILRANLQKGE1622 NPSHYGITAF 1632 NHPLNLTKQQ1642 LSEVALMTTS1652 VDVLVSICVI1662 FAMSFVPASF1672 VVFLIQERVS 1682 KAKHLQFISG1692 VKPVIYWLSN1702 FVWDMCNYVV1712 PATLVIIIFI1722 CFQQKSYVSS 1732 TNLPVLALLL1742 LLYGWSITPL1752 MYPASFVFKI1762 PSTAYVVLTS1772 VNLFIGINGS 1782 VATFVLELFT1792 DNKLNNINDI1802 LKSVFLIFPH1812 FCLGRGLIDM1822 VKNQAMADAL 1832 ERVSPLSWDL1848 VGRNLFAMAV1858 EGVVFFLITV1868 LIQYRFFIDE1891 DEDVRRERQR 1901 ILDGGGQNDI1911 LEIKELTKIY1921 RRKRKPAVDR1931 ICVGIPPGEC1941 FGLLGVNGAG 1951 KSSTFKMLTG1961 DTTVTRGDAF1971 LNKNSILSNI1981 HEVHQNMGYC1991 PQFDAITELL 2001 TGREHVEFFA2011 LLRGVPEKEV2021 GKVGEWAIRK2031 LGLVKYGEKY2041 AGNYSGGNKR 2051 KLSTAMALIG2061 GPPVVFLDQP2071 TTGMDPKARR2081 FLWNCALSVV2091 KEGRSVVLTS 2101 HSMEECEALC2111 TRMAIMVNGR2121 FRCLGSVQHL2131 KNRFGDGYTI2141 VVRIDLKPVQ 2156 DFFGLAFPGS2166 VLKEKHRNML2176 QYQLPSSLSS2186 LARIFSILSQ2196 SKKRLHIEDY 2206 SVSQTTLDQV2216 FVNFAKDQ
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TYR908
3.648
ASP910
3.086
LYS913
3.207
ALA915
3.874
GLY933
4.354
HIS934
3.932
ASN935
2.411
GLY936
3.425
ALA937
4.161
GLY938
3.076
LYS939
2.527
THR940
2.533
THR941
3.493
GLN980
2.742
LYS1025
3.106
GLN1032
1.296
SER1034
3.248
GLY1035
3.958
GLY1036
3.336
MET1037
4.445
ASP1057
4.966
GLN1058
3.964
GLY1062
3.839
HIS1089
2.575
TYR1921
3.593
LYS1924
2.849
ALA1928
4.056
GLY1946
4.886
VAL1947
4.284
ASN1948
2.861
GLY1949
3.371
ALA1950
4.236
GLY1951
3.181
LYS1952
2.963
SER1953
2.561
SER1954
2.840
THR1955
4.902
GLN1993
2.875
TYR2037
3.931
LYS2040
4.963
ASN2044
3.043
TYR2045
4.678
SER2046
3.231
GLY2047
3.144
GLY2048
2.580
ASN2049
4.905
GLN2070
2.791
GLY2074
2.852
MET2075
4.617
HIS2102
3.315
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| Ligand Name: Cholesterol | Ligand Info | |||||
| Structure Description | The structure of ATP-bound ABCA1 | PDB:7TBW | ||||
| Method | Electron microscopy | Resolution | 3.10 Å | Mutation | Yes | [7] |
| PDB Sequence |
CWPQLRLLLW
12 KNLTFRRRQT22 CQLLLEVAWP32 LFIFLILISV42 RLSYPPYEQH52 ECHFPNKAMP 62 SAGTLPWVQG72 IICNANNPCF82 RYPTPGEAPG92 VVGNFNKSIV102 ARLFSDARRL 112 LLYSQKDTSM122 KDMRKVLRTL132 QQIKKSSSKS200 EEMIQLGDQE210 VSELCGLPRE 220 KLAAAERVLR230 SNMDILKPIL240 RTLNSTSPFP250 SKELAEATKT260 LLHSLGTLAQ 270 ELFSMRSWSD280 MRQEVMFLTS296 STQIYQAVSR306 IVCGHTPYCN356 DLMKNLESSP 366 LSRIIWKALK376 PLLVGKILYT386 PDTPATRQVM396 AEVNKTFQEL406 AVFHDLEGMW 416 EELSPKIWTF426 MENSQEMDLV436 RMLLDSRDND446 HFWEQQLDGL456 DWTAQDIVAF 466 LAKHPVYTWR485 EAFNETNQAI495 RTISRFMECV505 NLNKLEPIAT515 EVWLINKSME 525 LLDERKFWAG535 IVFTGITPGS545 IELPHHVKYK555 IRMDIDNVER565 TNKIKDGYWD 575 PGPRADPFED585 MRYVWGGFAY595 LQDVVEQAII605 RVLTGTEKKT615 GVYMQQMPYP 625 CYVDDIFLRV635 MSRSMPLFMT645 LAWIYSVAVI655 IKGIVYEKEA665 RLKETMRIMG 675 LDNSILWFSW685 FISSLIPLLV695 SAGLLVVILK705 LGNLLPYSDP715 SVVFVFLSVF 725 AVVTILQCFL735 ISTLFSRANL745 AAACGGIIYF755 TLYLPYVLCV765 AWRDYVGFTL 775 KIFASLLSPV785 AFGFGCEYFA795 LFEEQGIGVQ805 WDNLFESPVE815 EDGFNLTTSV 825 SMMLFDTFLY835 GVMTWYIEAV845 FPGQYGIPRP855 WYFPCEPTHL895 KLGVSIQNLV 905 KVYRDGMKVA915 VDGLALNFYE925 GQITSFLGHN935 GAGKTTTMSI945 LTGLFPPTSG 955 TAYILGKDIR965 SEMSTIRQNL975 GVCPQHNVLF985 DMLTVEEHIW995 FYARLKGLSE 1005 KHVKAEMEQM1015 ALDVGLPSSK1025 LKSKTSQLSG1035 GMQRKLSVAL1045 AFVGGSKVVI 1055 LDQPTAGVDP1065 YSRRGIWELL1075 LKYRQGRTII1085 LSTHHMDEAD1095 VLGDRIAIIS 1105 HGKLCCVGSS1115 LFLKNQLGTG1125 YYLTLVKSAI1183 SNLIRKHVSE1193 ARLVEDIGHE 1203 LTYVLPAFVE1220 LFHEIDDRIS1235 SYGISETTLE1245 EIFLKVAEES1255 GKGSYQVKGW 1322 KLTQQQFVAL1332 LWKRLLIARR1342 SRKGFFAQIV1352 LPAVFVCIAL1362 VFSLIVPPFG 1372 KYPSLELQPW1382 MYNEQYTFVS1392 NDAPEDTGTL1402 ELLNALTKDP1412 GFGTRCMEGN 1422 PIPDTPCQAG1432 EEEWTTAPVP1442 QTIMDLFQNG1452 NWTMQNPSPA1462 CQCSKMLPVC 1477 PPGAGGLPPP1487 QRKQNTADIL1497 QDLTGRNISD1507 YLVKTYVQII1517 AKSLKNKIWV 1527 NEFRYGGFSL1537 GVSNPSQEVN1552 DAIKQMKKHL1562 KLAKDSSADR1572 FLNSLGRFMT 1582 GLDTKNNVKV1592 WFNNKGWHAI1602 SSFLNVINNA1612 ILRANLQKGE1622 NPSHYGITAF 1632 NHPLNLTKQQ1642 LSEVALMTTS1652 VDVLVSICVI1662 FAMSFVPASF1672 VVFLIQERVS 1682 KAKHLQFISG1692 VKPVIYWLSN1702 FVWDMCNYVV1712 PATLVIIIFI1722 CFQQKSYVSS 1732 TNLPVLALLL1742 LLYGWSITPL1752 MYPASFVFKI1762 PSTAYVVLTS1772 VNLFIGINGS 1782 VATFVLELFT1792 DNKLNNINDI1802 LKSVFLIFPH1812 FCLGRGLIDM1822 VKNQAMADAL 1832 ERVSPLSWDL1848 VGRNLFAMAV1858 EGVVFFLITV1868 LIQYRFFIDE1891 DEDVRRERQR 1901 ILDGGGQNDI1911 LEIKELTKIY1921 RRKRKPAVDR1931 ICVGIPPGEC1941 FGLLGVNGAG 1951 KSSTFKMLTG1961 DTTVTRGDAF1971 LNKNSILSNI1981 HEVHQNMGYC1991 PQFDAITELL 2001 TGREHVEFFA2011 LLRGVPEKEV2021 GKVGEWAIRK2031 LGLVKYGEKY2041 AGNYSGGNKR 2051 KLSTAMALIG2061 GPPVVFLDQP2071 TTGMDPKARR2081 FLWNCALSVV2091 KEGRSVVLTS 2101 HSMEECEALC2111 TRMAIMVNGR2121 FRCLGSVQHL2131 KNRFGDGYTI2141 VVRIDLKPVQ 2156 DFFGLAFPGS2166 VLKEKHRNML2176 QYQLPSSLSS2186 LARIFSILSQ2196 SKKRLHIEDY 2206 SVSQTTLDQV2216 FVNFAKDQ
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Click to View More Binding Site Information of This Target with Different Ligands | ||||||
| Different Human System Profiles of Target | Top |
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Human Similarity Proteins
of target is determined by comparing the sequence similarity of all human proteins with the target based on BLAST. The similarity proteins for a target are defined as the proteins with E-value < 0.005 and outside the protein families of the target.
A target that has fewer human similarity proteins outside its family is commonly regarded to possess a greater capacity to avoid undesired interactions and thus increase the possibility of finding successful drugs
(Brief Bioinform, 21: 649-662, 2020).
Human Tissue Distribution
of target is determined from a proteomics study that quantified more than 12,000 genes across 32 normal human tissues. Tissue Specificity (TS) score was used to define the enrichment of target across tissues.
The distribution of targets among different tissues or organs need to be taken into consideration when assessing the target druggability, as it is generally accepted that the wider the target distribution, the greater the concern over potential adverse effects
(Nat Rev Drug Discov, 20: 64-81, 2021).
Human Pathway Affiliation
of target is determined by the life-essential pathways provided on KEGG database. The target-affiliated pathways were defined based on the following two criteria (a) the pathways of the studied target should be life-essential for both healthy individuals and patients, and (b) the studied target should occupy an upstream position in the pathways and therefore had the ability to regulate biological function.
Targets involved in a fewer pathways have greater likelihood to be successfully developed, while those associated with more human pathways increase the chance of undesirable interferences with other human processes
(Pharmacol Rev, 58: 259-279, 2006).
Biological Network Descriptors
of target is determined based on a human protein-protein interactions (PPI) network consisting of 9,309 proteins and 52,713 PPIs, which were with a high confidence score of ≥ 0.95 collected from STRING database.
The network properties of targets based on protein-protein interactions (PPIs) have been widely adopted for the assessment of target’s druggability. Proteins with high node degree tend to have a high impact on network function through multiple interactions, while proteins with high betweenness centrality are regarded to be central for communication in interaction networks and regulate the flow of signaling information
(Front Pharmacol, 9, 1245, 2018;
Curr Opin Struct Biol. 44:134-142, 2017).
Human Similarity Proteins
Human Tissue Distribution
Human Pathway Affiliation
Biological Network Descriptors
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There is no similarity protein (E value < 0.005) for this target
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Note:
If a protein has TS (tissue specficity) scores at least in one tissue >= 2.5, this protein is called tissue-enriched (including tissue-enriched-but-not-specific and tissue-specific). In the plots, the vertical lines are at thresholds 2.5 and 4.
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| KEGG Pathway | Pathway ID | Affiliated Target | Pathway Map |
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| ABC transporters | hsa02010 | Affiliated Target |
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| Class: Environmental Information Processing => Membrane transport | Pathway Hierarchy | ||
| Fat digestion and absorption | hsa04975 | Affiliated Target |
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| Class: Organismal Systems => Digestive system | Pathway Hierarchy | ||
| Cholesterol metabolism | hsa04979 | Affiliated Target |
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| Class: Organismal Systems => Digestive system | Pathway Hierarchy | ||
| Degree | 6 | Degree centrality | 6.45E-04 | Betweenness centrality | 9.15E-05 |
|---|---|---|---|---|---|
| Closeness centrality | 2.10E-01 | Radiality | 1.37E+01 | Clustering coefficient | 4.00E-01 |
| Neighborhood connectivity | 2.78E+01 | Topological coefficient | 2.39E-01 | Eccentricity | 11 |
| Download | Click to Download the Full PPI Network of This Target | ||||
| Co-Targets | Top | |||||
|---|---|---|---|---|---|---|
| Co-Targets | ||||||
| Target Regulators | Top | |||||
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| Target-regulating microRNAs | ||||||
| Target-interacting Proteins | ||||||
| Target Profiles in Patients | Top | |||||
|---|---|---|---|---|---|---|
| Target Expression Profile (TEP) | ||||||
| Target Affiliated Biological Pathways | Top | |||||
|---|---|---|---|---|---|---|
| KEGG Pathway | [+] 2 KEGG Pathways | + | ||||
| 1 | ABC transporters | |||||
| 2 | Fat digestion and absorption | |||||
| NetPath Pathway | [+] 1 NetPath Pathways | + | ||||
| 1 | Leptin Signaling Pathway | |||||
| PID Pathway | [+] 1 PID Pathways | + | ||||
| 1 | RXR and RAR heterodimerization with other nuclear receptor | |||||
| Reactome | [+] 2 Reactome Pathways | + | ||||
| 1 | HDL-mediated lipid transport | |||||
| 2 | PPARA activates gene expression | |||||
| WikiPathways | [+] 8 WikiPathways | + | ||||
| 1 | Statin Pathway | |||||
| 2 | Nuclear Receptors in Lipid Metabolism and Toxicity | |||||
| 3 | Regulation of Lipid Metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha) | |||||
| 4 | Lipid digestion, mobilization, and transport | |||||
| 5 | SREBF and miR33 in cholesterol and lipid homeostasis | |||||
| 6 | Folate Metabolism | |||||
| 7 | Vitamin B12 Metabolism | |||||
| 8 | Selenium Micronutrient Network | |||||
| References | Top | |||||
|---|---|---|---|---|---|---|
| REF 1 | Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. | |||||
| REF 2 | URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 7277). | |||||
| REF 3 | FDA Approved Drug Products from FDA Official Website. 2009. Application Number: (NDA) 017535. | |||||
| REF 4 | Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800031594) | |||||
| REF 5 | URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 756). | |||||
| REF 6 | Analysis of "On/Off" Kinetics of a CETP Inhibitor Using a Mechanistic Model of Lipoprotein Metabolism and Kinetics. CPT Pharmacometrics Syst Pharmacol. 2015 Aug;4(8):465-73. | |||||
| REF 7 | Cholesterol efflux mechanism revealed by structural analysis of human ABCA1 conformational states. Nat Cardiovasc Res. 2022;1(3):238-245. | |||||
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