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P41233

- ABCA1_MOUSE

UniProt

P41233 - ABCA1_MOUSE

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Protein

ATP-binding cassette sub-family A member 1

Gene

Abca1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

cAMP-dependent and sulfonylurea-sensitive anion transporter. Key gatekeeper influencing intracellular cholesterol transport (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi933 – 9408ATP 1PROSITE-ProRule annotation
Nucleotide bindingi1946 – 19538ATP 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. anion transmembrane transporter activity Source: BHF-UCL
  2. apolipoprotein A-I receptor activity Source: Ensembl
  3. ATPase activity Source: InterPro
  4. ATP binding Source: UniProtKB-KW
  5. cholesterol transporter activity Source: MGI
  6. phospholipid transporter activity Source: MGI

GO - Biological processi

  1. cellular response to cholesterol Source: Ensembl
  2. cellular response to lipopolysaccharide Source: UniProtKB
  3. cellular response to retinoic acid Source: UniProtKB
  4. cholesterol efflux Source: MGI
  5. cholesterol homeostasis Source: Ensembl
  6. cholesterol metabolic process Source: MGI
  7. endosomal transport Source: Ensembl
  8. G-protein coupled receptor signaling pathway Source: Ensembl
  9. high-density lipoprotein particle assembly Source: Ensembl
  10. interleukin-1 beta secretion Source: Ensembl
  11. intracellular cholesterol transport Source: Ensembl
  12. lipoprotein biosynthetic process Source: MGI
  13. lipoprotein metabolic process Source: MGI
  14. lysosome organization Source: Ensembl
  15. peptide secretion Source: MGI
  16. phagocytosis, engulfment Source: MGI
  17. phospholipid efflux Source: MGI
  18. phospholipid homeostasis Source: Ensembl
  19. phospholipid translocation Source: MGI
  20. platelet dense granule organization Source: Ensembl
  21. positive regulation of cAMP biosynthetic process Source: Ensembl
  22. positive regulation of cholesterol efflux Source: BHF-UCL
  23. protein lipidation Source: MGI
  24. regulation of Cdc42 protein signal transduction Source: Ensembl
  25. response to drug Source: Ensembl
  26. response to laminar fluid shear stress Source: Ensembl
  27. response to low-density lipoprotein particle Source: Ensembl
  28. response to nutrient Source: Ensembl
  29. reverse cholesterol transport Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198602. PPARA activates gene expression.
REACT_213857. HDL-mediated lipid transport.

Protein family/group databases

TCDBi3.A.1.211.1. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-binding cassette sub-family A member 1
Alternative name(s):
ATP-binding cassette transporter 1
Short name:
ABC-1
Short name:
ATP-binding cassette 1
Gene namesi
Name:Abca1
Synonyms:Abc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:99607. Abca1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei22 – 4221HelicalSequence AnalysisAdd
BLAST
Topological domaini43 – 639597ExtracellularBy similarityAdd
BLAST
Transmembranei640 – 66021HelicalSequence AnalysisAdd
BLAST
Transmembranei683 – 70321HelicalSequence AnalysisAdd
BLAST
Transmembranei716 – 73621HelicalSequence AnalysisAdd
BLAST
Transmembranei745 – 76521HelicalSequence AnalysisAdd
BLAST
Transmembranei777 – 79721HelicalSequence AnalysisAdd
BLAST
Transmembranei827 – 84721HelicalSequence AnalysisAdd
BLAST
Transmembranei941 – 96121HelicalSequence AnalysisAdd
BLAST
Transmembranei1351 – 137121HelicalSequence AnalysisAdd
BLAST
Topological domaini1372 – 1656285ExtracellularBy similarityAdd
BLAST
Transmembranei1657 – 167721HelicalSequence AnalysisAdd
BLAST
Transmembranei1703 – 172321HelicalSequence AnalysisAdd
BLAST
Transmembranei1735 – 175521HelicalSequence AnalysisAdd
BLAST
Transmembranei1768 – 178821HelicalSequence AnalysisAdd
BLAST
Transmembranei1802 – 182221HelicalSequence AnalysisAdd
BLAST
Transmembranei1852 – 187221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: MGI
  2. Golgi apparatus Source: MGI
  3. integral component of plasma membrane Source: MGI
  4. intracellular membrane-bounded organelle Source: MGI
  5. membrane raft Source: Ensembl
  6. perinuclear region of cytoplasm Source: Ensembl
  7. phagocytic vesicle Source: Ensembl
  8. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22612261ATP-binding cassette sub-family A member 1PRO_0000093289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi3 – 31S-palmitoyl cysteineBy similarity
Glycosylationi14 – 141N-linked (GlcNAc...)Sequence Analysis
Lipidationi23 – 231S-palmitoyl cysteineBy similarity
Disulfide bondi75 ↔ 309By similarity
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi489 – 4891N-linked (GlcNAc...)1 Publication
Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi820 – 8201N-linked (GlcNAc...)Sequence Analysis
Modified residuei1042 – 10421Phosphoserine; by PKABy similarity
Lipidationi1110 – 11101S-palmitoyl cysteineBy similarity
Lipidationi1111 – 11111S-palmitoyl cysteineBy similarity
Glycosylationi1144 – 11441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1294 – 12941N-linked (GlcNAc...)Sequence Analysis
Modified residuei1296 – 12961Phosphoserine1 Publication
Glycosylationi1453 – 14531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1463 ↔ 1477By similarity
Glycosylationi1499 – 14991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1504 – 15041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1637 – 16371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2044 – 20441N-linked (GlcNAc...)Sequence Analysis
Modified residuei2054 – 20541Phosphoserine; by PKABy similarity
Glycosylationi2238 – 22381N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Phosphorylation on Ser-2054 regulates phospholipid efflux.By similarity
Palmitoylation by DHHC8 is essential for membrane localization.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP41233.
PaxDbiP41233.
PRIDEiP41233.

PTM databases

PhosphoSiteiP41233.

Miscellaneous databases

PMAP-CutDBB1AWZ8.

Expressioni

Tissue specificityi

Widely expressed in adult tissues. Highest levels are found in pregnant uterus and uterus.

Inductioni

Down-regulated by endotoxins (LPS) or cytokines (TNF and IL-1) in J774 macrophages. The down-regulation by endotoxin in macrophages is not likely to be mediated by the liver X receptor/retinoic X receptor (LXR/RXR).1 Publication

Gene expression databases

BgeeiP41233.
GenevestigatoriP41233.

Interactioni

Subunit structurei

Interacts with MEGF10.1 Publication

Protein-protein interaction databases

BioGridi197900. 2 interactions.
IntActiP41233. 2 interactions.
STRINGi10090.ENSMUSP00000030010.

Structurei

3D structure databases

ProteinModelPortaliP41233.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini899 – 1131233ABC transporter 1PROSITE-ProRule annotationAdd
BLAST
Domaini1912 – 2144233ABC transporter 2PROSITE-ProRule annotationAdd
BLAST

Domaini

Multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain.

Sequence similaritiesi

Contains 2 ABC transporter domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1131.
GeneTreeiENSGT00760000118965.
HOGENOMiHOG000231547.
HOVERGENiHBG050436.
InParanoidiP41233.
KOiK05641.
OMAiFSMRSWS.
OrthoDBiEOG78D7J6.
TreeFamiTF105191.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR026082. ABC_A.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR19229. PTHR19229. 1 hit.
PfamiPF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41233-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE
60 70 80 90 100
QHECHFPNKA MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS
110 120 130 140 150
IVSRLFSDAQ RLLLYSQRDT SIKDMHKVLR MLRQIKHPNS NLKLQDFLVD
160 170 180 190 200
NETFSGFLQH NLSLPRSTVD SLLQANVGLQ KVFLQGYQLH LASLCNGSKL
210 220 230 240 250
EEIIQLGDAE VSALCGLPRK KLDAAERVLR YNMDILKPVV TKLNSTSHLP
260 270 280 290 300
TQHLAEATTV LLDSLGGLAQ ELFSTKSWSD MRQEVMFLTN VNSSSSSTQI
310 320 330 340 350
YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNNTE EDVDTFYDNS
360 370 380 390 400
TTPYCNDLMK NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN
410 420 430 440 450
KTFQELAVFH DLEGMWEELS PQIWTFMENS QEMDLVRTLL DSRGNDQFWE
460 470 480 490 500
QKLDGLDWTA QDIMAFLAKN PEDVQSPNGS VYTWREAFNE TNQAIQTISR
510 520 530 540 550
FMECVNLNKL EPIPTEVRLI NKSMELLDER KFWAGIVFTG ITPDSVELPH
560 570 580 590 600
HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV
610 620 630 640 650
EQAIIRVLTG SEKKTGVYVQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY
660 670 680 690 700
SVAVIIKSIV YEKEARLKET MRIMGLDNGI LWFSWFVSSL IPLLVSAGLL
710 720 730 740 750
VVILKLGNLL PYSDPSVVFV FLSVFAMVTI LQCFLISTLF SRANLAAACG
760 770 780 790 800
GIIYFTLYLP YVLCVAWQDY VGFSIKIFAS LLSPVAFGFG CEYFALFEEQ
810 820 830 840 850
GIGVQWDNLF ESPVEEDGFN LTTAVSMMLF DTFLYGVMTW YIEAVFPGQY
860 870 880 890 900
GIPRPWYFPC TKSYWFGEEI DEKSHPGSSQ KGVSEICMEE EPTHLRLGVS
910 920 930 940 950
IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF
960 970 980 990 1000
PPTSGTAYIL GKDIRSEMSS IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL
1010 1020 1030 1040 1050
KGLSEKHVKA EMEQMALDVG LPPSKLKSKT SQLSGGMQRK LSVALAFVGG
1060 1070 1080 1090 1100
SKVVILDEPT AGVDPYSRRG IWELLLKYRQ GRTIILSTHH MDEADILGDR
1110 1120 1130 1140 1150
IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS SCRNSSSTVS
1160 1170 1180 1190 1200
CLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI
1210 1220 1230 1240 1250
GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK
1260 1270 1280 1290 1300
VAEESGVDAE TSDGTLPARR NRRAFGDKQS CLHPFTEDDA VDPNDSDIDP
1310 1320 1330 1340 1350
ESRETDLLSG MDGKGSYQLK GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ
1360 1370 1380 1390 1400
IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ PWMYNEQYTF VSNDAPEDMG
1410 1420 1430 1440 1450
TQELLNALTK DPGFGTRCME GNPIPDTPCL AGEEDWTISP VPQSIVDLFQ
1460 1470 1480 1490 1500
NGNWTMKNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QKTADILQNL
1510 1520 1530 1540 1550
TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NSQALPPSHE
1560 1570 1580 1590 1600
VNDAIKQMKK LLKLTKDSSA DRFLSSLGRF MAGLDTKNNV KVWFNNKGWH
1610 1620 1630 1640 1650
AISSFLNVIN NAILRANLQK GENPSQYGIT AFNHPLNLTK QQLSEVALMT
1660 1670 1680 1690 1700
TSVDVLVSIC VIFAMSFVPA SFVVFLIQER VSKAKHLQFI SGVKPVIYWL
1710 1720 1730 1740 1750
SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL LLLLYGWSIT
1760 1770 1780 1790 1800
PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTNNKLNDIN
1810 1820 1830 1840 1850
DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG
1860 1870 1880 1890 1900
RNLFAMAVEG VVFFLITVLI QYRFFIRPRP VKAKLPPLND EDEDVRRERQ
1910 1920 1930 1940 1950
RILDGGGQND ILEIKELTKI YRRKRKPAVD RICIGIPPGE CFGLLGVNGA
1960 1970 1980 1990 2000
GKSTTFKMLT GDTPVTRGDA FLNKNSILSN IHEVHQNMGY CPQFDAITEL
2010 2020 2030 2040 2050
LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK YASNYSGGNK
2060 2070 2080 2090 2100
RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSI VKEGRSVVLT
2110 2120 2130 2140 2150
SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP
2160 2170 2180 2190 2200
DLKPVQEFFG LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR
2210 2220 2230 2240 2250
LHIEDYSVSQ TTLDQVFVNF AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF
2260
LQDEKVKESY V
Length:2,261
Mass (Da):253,912
Last modified:July 27, 2011 - v4
Checksum:iE041DA4FA73C2660
GO

Sequence cautioni

The sequence AAG39073.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA53530.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1567 – 15682Missing in AAG39073. (PubMed:11352567)Curated
Sequence conflicti1568 – 15681S → T in CAA53530. (PubMed:8088782)Curated
Sequence conflicti2024 – 20241V → F in CAA53530. (PubMed:8088782)Curated
Sequence conflicti2024 – 20241Missing in AAG39073. (PubMed:11352567)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75926 mRNA. Translation: CAA53530.1. Different initiation.
AF287263 Genomic DNA. Translation: AAG39073.1. Different initiation.
AL807243, AL772397 Genomic DNA. Translation: CAM18883.1.
AL772397, AL807243 Genomic DNA. Translation: CAM27437.1.
CH466565 Genomic DNA. Translation: EDL02285.1.
CCDSiCCDS18187.1.
PIRiA54774.
RefSeqiNP_038482.3. NM_013454.3.
UniGeneiMm.277376.

Genome annotation databases

EnsembliENSMUST00000030010; ENSMUSP00000030010; ENSMUSG00000015243.
GeneIDi11303.
KEGGimmu:11303.
UCSCiuc008swu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75926 mRNA. Translation: CAA53530.1 . Different initiation.
AF287263 Genomic DNA. Translation: AAG39073.1 . Different initiation.
AL807243 , AL772397 Genomic DNA. Translation: CAM18883.1 .
AL772397 , AL807243 Genomic DNA. Translation: CAM27437.1 .
CH466565 Genomic DNA. Translation: EDL02285.1 .
CCDSi CCDS18187.1.
PIRi A54774.
RefSeqi NP_038482.3. NM_013454.3.
UniGenei Mm.277376.

3D structure databases

ProteinModelPortali P41233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 197900. 2 interactions.
IntActi P41233. 2 interactions.
STRINGi 10090.ENSMUSP00000030010.

Chemistry

ChEMBLi CHEMBL1641361.

Protein family/group databases

TCDBi 3.A.1.211.1. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSitei P41233.

Proteomic databases

MaxQBi P41233.
PaxDbi P41233.
PRIDEi P41233.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030010 ; ENSMUSP00000030010 ; ENSMUSG00000015243 .
GeneIDi 11303.
KEGGi mmu:11303.
UCSCi uc008swu.1. mouse.

Organism-specific databases

CTDi 19.
MGIi MGI:99607. Abca1.

Phylogenomic databases

eggNOGi COG1131.
GeneTreei ENSGT00760000118965.
HOGENOMi HOG000231547.
HOVERGENi HBG050436.
InParanoidi P41233.
KOi K05641.
OMAi FSMRSWS.
OrthoDBi EOG78D7J6.
TreeFami TF105191.

Enzyme and pathway databases

Reactomei REACT_198602. PPARA activates gene expression.
REACT_213857. HDL-mediated lipid transport.

Miscellaneous databases

NextBioi 278586.
PMAP-CutDB B1AWZ8.
PROi P41233.
SOURCEi Search...

Gene expression databases

Bgeei P41233.
Genevestigatori P41233.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR026082. ABC_A.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR19229. PTHR19229. 1 hit.
Pfami PF00005. ABC_tran. 2 hits.
[Graphical view ]
SMARTi SM00382. AAA. 2 hits.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of two novel ABC transporters mapping on human chromosome 9."
    Luciani M.-F., Denizot F., Savary S., Mattei M.-G., Chimini G.
    Genomics 21:150-159(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DBA/2.
    Tissue: Macrophage.
  2. "Human and mouse ABCA1 comparative sequencing and transgenesis studies revealing novel regulatory sequences."
    Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F.
    Genomics 73:66-76(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6J.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Bacterial lipopolysaccharide induces expression of ABCA1 but not ABCG1 via an LXR-independent pathway."
    Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.
    J. Lipid Res. 43:952-959(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY LIPOPOLYSACCHARIDE.
  6. "Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and ABCG1 in J774 murine macrophages: differential role of LXR."
    Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C., Feingold K.R.
    J. Lipid Res. 44:1728-1736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION BY ENDOTOXIN.
  7. "Cooperation between engulfment receptors: the case of ABCA1 and MEGF10."
    Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V., Zhou Z., Chimini G.
    PLoS ONE 1:E120-E120(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEGF10.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-489.

Entry informationi

Entry nameiABCA1_MOUSE
AccessioniPrimary (citable) accession number: P41233
Secondary accession number(s): B1AWZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 145 of the entry and version 4 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