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P33527 (MRP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multidrug resistance-associated protein 1
Alternative name(s):
ATP-binding cassette sub-family C member 1
Leukotriene C(4) transporter
Short name=LTC4 transporter
Gene names
Name:ABCC1
Synonyms:MRP, MRP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1531 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs. Hydrolyzes ATP with low efficiency. Ref.11 Ref.12 Ref.19

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.19.

Tissue specificity

Lung, testis and peripheral blood mononuclear cells.

Sequence similarities

Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. [View classification]

Contains 2 ABC transmembrane type-1 domains.

Contains 2 ABC transporter domains.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 15999530. Source: GOC

arachidonic acid metabolic process

Traceable author statement. Source: Reactome

cobalamin metabolic process

Traceable author statement. Source: Reactome

leukotriene metabolic process

Traceable author statement. Source: Reactome

response to drug

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

vitamin metabolic process

Traceable author statement. Source: Reactome

water-soluble vitamin metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Traceable author statement Ref.1. Source: ProtInc

ATPase activity

Inferred from direct assay PubMed 15999530. Source: UniProtKB

ATPase activity, coupled to transmembrane movement of substances

Traceable author statement Ref.1. Source: ProtInc

transporter activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: P33527-1)

Also known as: Allexons;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P33527-2)

Also known as: Delexon-17;

The sequence of this isoform differs from the canonical sequence as follows:
     706-764: Missing.
Isoform 3 (identifier: P33527-3)

Also known as: Delexon-18;

The sequence of this isoform differs from the canonical sequence as follows:
     765-820: Missing.
Isoform 4 (identifier: P33527-4)

Also known as: Delexon-30;

The sequence of this isoform differs from the canonical sequence as follows:
     1431-1495: Missing.
Isoform 5 (identifier: P33527-5)

Also known as: Delexon-17-18;

The sequence of this isoform differs from the canonical sequence as follows:
     706-764: Missing.
     765-820: Missing.
Isoform 6 (identifier: P33527-6)

Also known as: Delexon-17-30;

The sequence of this isoform differs from the canonical sequence as follows:
     706-764: Missing.
     1431-1495: Missing.
Isoform 7 (identifier: P33527-7)

Also known as: Delexon-18-30;

The sequence of this isoform differs from the canonical sequence as follows:
     765-820: Missing.
     1431-1495: Missing.
Isoform 8 (identifier: P33527-8)

Also known as: Delexon-17-18-30;

The sequence of this isoform differs from the canonical sequence as follows:
     706-764: Missing.
     765-820: Missing.
     1431-1495: Missing.
Isoform 9 (identifier: P33527-9)

The sequence of this isoform differs from the canonical sequence as follows:
     882-882: G → GSTVMDEEEAG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15311531Multidrug resistance-associated protein 1
PRO_0000093351

Regions

Topological domain1 – 3333Extracellular Ref.8 Ref.9 Ref.10
Transmembrane34 – 5421Helical; Name=1
Topological domain55 – 7420Cytoplasmic Ref.8 Ref.9 Ref.10
Transmembrane75 – 9521Helical; Name=2
Topological domain96 – 1005Extracellular Ref.8 Ref.9 Ref.10
Transmembrane101 – 12121Helical; Name=3
Topological domain122 – 13312Cytoplasmic Ref.8 Ref.9 Ref.10
Transmembrane134 – 15421Helical; Name=4
Topological domain155 – 17218Extracellular Ref.8 Ref.9 Ref.10
Transmembrane173 – 19321Helical; Name=5
Topological domain194 – 316123Cytoplasmic Ref.8 Ref.9 Ref.10
Transmembrane317 – 33721Helical; Name=6
Topological domain338 – 36326Extracellular Ref.8 Ref.9 Ref.10
Transmembrane364 – 38421Helical; Name=7
Topological domain385 – 44056Cytoplasmic Ref.8 Ref.9 Ref.10
Transmembrane441 – 46121Helical; Name=8
Topological domain462 – 4643Extracellular Ref.8 Ref.9 Ref.10
Transmembrane465 – 48521Helical; Name=9
Topological domain486 – 54762Cytoplasmic Ref.8 Ref.9 Ref.10
Transmembrane548 – 56821Helical; Name=10
Topological domain569 – 59022Extracellular Ref.8 Ref.9 Ref.10
Transmembrane591 – 61121Helical; Name=11
Topological domain612 – 967356Cytoplasmic Ref.8 Ref.9 Ref.10
Transmembrane968 – 98821Helical; Name=12
Topological domain989 – 102537Extracellular Ref.8 Ref.9 Ref.10
Transmembrane1026 – 104621Helical; Name=13
Topological domain1047 – 108943Cytoplasmic Ref.8 Ref.9 Ref.10
Transmembrane1090 – 111021Helical; Name=14
Topological domain11111Extracellular Ref.8 Ref.9 Ref.10
Transmembrane1112 – 113221Helical; Name=15
Topological domain1133 – 120371Cytoplasmic Ref.8 Ref.9 Ref.10
Transmembrane1204 – 122421Helical; Name=16
Topological domain1225 – 12262Extracellular Ref.8 Ref.9 Ref.10
Transmembrane1227 – 124721Helical; Name=17
Topological domain1248 – 1531284Cytoplasmic Ref.8 Ref.9 Ref.10
Domain325 – 608284ABC transmembrane type-1 1
Domain644 – 868225ABC transporter 1
Domain975 – 1256282ABC transmembrane type-1 2
Domain1293 – 1527235ABC transporter 2
Nucleotide binding678 – 6858ATP 1
Nucleotide binding1327 – 13348ATP 2 Potential

Sites

Binding site6531ATP 1
Binding site7131ATP 1

Amino acid modifications

Modified residue5031N6-succinyllysine By similarity
Modified residue9051Phosphoserine Ref.23
Modified residue9151Phosphoserine Ref.22
Modified residue9301Phosphoserine Ref.23 Ref.25
Glycosylation191N-linked (GlcNAc...) Ref.8
Glycosylation231N-linked (GlcNAc...) Ref.8
Glycosylation10061N-linked (GlcNAc...) Ref.8

Natural variations

Alternative sequence706 – 76459Missing in isoform 2, isoform 5, isoform 6 and isoform 8.
VSP_000037
Alternative sequence765 – 82056Missing in isoform 3, isoform 5, isoform 7 and isoform 8.
VSP_000038
Alternative sequence8821G → GSTVMDEEEAG in isoform 9.
VSP_017014
Alternative sequence1431 – 149565Missing in isoform 4, isoform 6, isoform 7 and isoform 8.
VSP_000039
Natural variant431C → S. Ref.31
Corresponds to variant rs41395947 [ dbSNP | Ensembl ].
VAR_013317
Natural variant731T → I. Ref.31
Corresponds to variant rs41494447 [ dbSNP | Ensembl ].
VAR_013318
Natural variant1171M → T. Ref.1 Ref.3 Ref.30
VAR_013319
Natural variant4331R → S. Ref.29 Ref.32
Corresponds to variant rs60782127 [ dbSNP | Ensembl ].
VAR_013320
Natural variant6331R → Q. Ref.27
Corresponds to variant rs112282109 [ dbSNP | Ensembl ].
VAR_011488
Natural variant6711G → V No effect on leukotriene C4 and estradiol glucuronide transport. Ref.4 Ref.27 Ref.28 Ref.29
Corresponds to variant rs45511401 [ dbSNP | Ensembl ].
VAR_011489
Natural variant7231R → Q. Ref.4 Ref.31
Corresponds to variant rs4148356 [ dbSNP | Ensembl ].
VAR_013321
Natural variant8611A → T. Ref.4
Corresponds to variant rs45517537 [ dbSNP | Ensembl ].
VAR_055384
Natural variant10471C → S. Ref.4
Corresponds to variant rs13337489 [ dbSNP | Ensembl ].
VAR_055385
Natural variant10581R → Q. Ref.31
Corresponds to variant rs41410450 [ dbSNP | Ensembl ].
VAR_013322
Natural variant11461V → I. Ref.4
Corresponds to variant rs28706727 [ dbSNP | Ensembl ].
VAR_055386
Natural variant15121S → L. Ref.30
VAR_013323

Experimental info

Mutagenesis5801Q → A: No effect. Ref.17
Mutagenesis5811T → A: No effect. Ref.17
Mutagenesis5851S → A: No effect. Ref.17
Mutagenesis5971N → A: Increases resistance to vincristine and decreases resistance to VP-16. Ref.17
Mutagenesis6041S → A: Increases estradiol glucuronide transport. Ref.17
Mutagenesis6051S → A: Decreases resistance to vincristine, VP-16 and doxorubicin. Ref.17
Mutagenesis7921D → A: Only partially affects protein maturation; impairs leukotriene C4 transport. Ref.13
Mutagenesis7921D → L: Impairs protein maturation and leukotriene C4 transport. Ref.13
Mutagenesis7931D → L: No effect on protein maturation and leukotriene C4 transport. Ref.13
Mutagenesis10461R → D: Slightly impairs leukotriene C4 and estradiol glucuronide transport. Ref.16
Mutagenesis10841D → R: Impairs leukotriene C4 and estradiol glucuronide transport. Ref.16
Mutagenesis10891E → A, L, N or Q: Decreases resistance to anthracyclines. Ref.15
Mutagenesis10891E → D: No effect. Ref.15
Mutagenesis10891E → K: Abolishes resistance to anthracyclines. Ref.15
Mutagenesis11311R → E: Slightly impairs leukotriene C4 and estradiol glucuronide transport. Ref.16
Mutagenesis11381R → E or K: Strongly reduced transport of leukotriene C4, estradiol glucuronide and of glutathione. Ref.19
Mutagenesis11411K → E: Reduced transport of leukotriene C4 and of glutathione. Ref.19
Mutagenesis11411K → R: Reduced transport of glutathione. Ref.19
Mutagenesis11421R → E or K: Reduced transport of leukotriene C4, estradiol glucuronide and of glutathione. Ref.19
Mutagenesis12461W → A, F or Y: Impairs estradiol glucuronide transport. Ref.14
Mutagenesis12461W → C: Impairs estradiol glucuronide transport; loss of resistance to alkaloid vincristine, cationic anthracyclines, epipodophyllotoxin VP-16, but not potassium antimony tartrate; partial loss of resistance to sodium arsenite. Ref.14
Mutagenesis13331K → L: Impairs leukotriene C4 transport. Ref.13
Mutagenesis1454 – 14552DE → LL: Impairs leukotriene C4 transport.

Secondary structure

.......................................... 1531
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Allexons) [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 46A7CB643B9478C4

FASTA1,531171,591
        10         20         30         40         50         60 
MALRGFCSAD GSDPLWDWNV TWNTSNPDFT KCFQNTVLVW VPCFYLWACF PFYFLYLSRH 

        70         80         90        100        110        120 
DRGYIQMTPL NKTKTALGFL LWIVCWADLF YSFWERSRGI FLAPVFLVSP TLLGITMLLA 

       130        140        150        160        170        180 
TFLIQLERRK GVQSSGIMLT FWLVALVCAL AILRSKIMTA LKEDAQVDLF RDITFYVYFS 

       190        200        210        220        230        240 
LLLIQLVLSC FSDRSPLFSE TIHDPNPCPE SSASFLSRIT FWWITGLIVR GYRQPLEGSD 

       250        260        270        280        290        300 
LWSLNKEDTS EQVVPVLVKN WKKECAKTRK QPVKVVYSSK DPAQPKESSK VDANEEVEAL 

       310        320        330        340        350        360 
IVKSPQKEWN PSLFKVLYKT FGPYFLMSFF FKAIHDLMMF SGPQILKLLI KFVNDTKAPD 

       370        380        390        400        410        420 
WQGYFYTVLL FVTACLQTLV LHQYFHICFV SGMRIKTAVI GAVYRKALVI TNSARKSSTV 

       430        440        450        460        470        480 
GEIVNLMSVD AQRFMDLATY INMIWSAPLQ VILALYLLWL NLGPSVLAGV AVMVLMVPVN 

       490        500        510        520        530        540 
AVMAMKTKTY QVAHMKSKDN RIKLMNEILN GIKVLKLYAW ELAFKDKVLA IRQEELKVLK 

       550        560        570        580        590        600 
KSAYLSAVGT FTWVCTPFLV ALCTFAVYVT IDENNILDAQ TAFVSLALFN ILRFPLNILP 

       610        620        630        640        650        660 
MVISSIVQAS VSLKRLRIFL SHEELEPDSI ERRPVKDGGG TNSITVRNAT FTWARSDPPT 

       670        680        690        700        710        720 
LNGITFSIPE GALVAVVGQV GCGKSSLLSA LLAEMDKVEG HVAIKGSVAY VPQQAWIQND 

       730        740        750        760        770        780 
SLRENILFGC QLEEPYYRSV IQACALLPDL EILPSGDRTE IGEKGVNLSG GQKQRVSLAR 

       790        800        810        820        830        840 
AVYSNADIYL FDDPLSAVDA HVGKHIFENV IGPKGMLKNK TRILVTHSMS YLPQVDVIIV 

       850        860        870        880        890        900 
MSGGKISEMG SYQELLARDG AFAEFLRTYA STEQEQDAEE NGVTGVSGPG KEAKQMENGM 

       910        920        930        940        950        960 
LVTDSAGKQL QRQLSSSSSY SGDISRHHNS TAELQKAEAK KEETWKLMEA DKAQTGQVKL 

       970        980        990       1000       1010       1020 
SVYWDYMKAI GLFISFLSIF LFMCNHVSAL ASNYWLSLWT DDPIVNGTQE HTKVRLSVYG 

      1030       1040       1050       1060       1070       1080 
ALGISQGIAV FGYSMAVSIG GILASRCLHV DLLHSILRSP MSFFERTPSG NLVNRFSKEL 

      1090       1100       1110       1120       1130       1140 
DTVDSMIPEV IKMFMGSLFN VIGACIVILL ATPIAAIIIP PLGLIYFFVQ RFYVASSRQL 

      1150       1160       1170       1180       1190       1200 
KRLESVSRSP VYSHFNETLL GVSVIRAFEE QERFIHQSDL KVDENQKAYY PSIVANRWLA 

      1210       1220       1230       1240       1250       1260 
VRLECVGNCI VLFAALFAVI SRHSLSAGLV GLSVSYSLQV TTYLNWLVRM SSEMETNIVA 

      1270       1280       1290       1300       1310       1320 
VERLKEYSET EKEAPWQIQE TAPPSSWPQV GRVEFRNYCL RYREDLDFVL RHINVTINGG 

      1330       1340       1350       1360       1370       1380 
EKVGIVGRTG AGKSSLTLGL FRINESAEGE IIIDGINIAK IGLHDLRFKI TIIPQDPVLF 

      1390       1400       1410       1420       1430       1440 
SGSLRMNLDP FSQYSDEEVW TSLELAHLKD FVSALPDKLD HECAEGGENL SVGQRQLVCL 

      1450       1460       1470       1480       1490       1500 
ARALLRKTKI LVLDEATAAV DLETDDLIQS TIRTQFEDCT VLTIAHRLNT IMDYTRVIVL 

      1510       1520       1530 
DKGEIQEYGA PSDLLQQRGL FYSMAKDAGL V 

« Hide

Isoform 2 (Delexon-17) [UniParc].

Checksum: 143FA6CB7F3123EF
Show »

FASTA1,472164,971
Isoform 3 (Delexon-18) [UniParc].

Checksum: F49C1B33B976D008
Show »

FASTA1,475165,569
Isoform 4 (Delexon-30) [UniParc].

Checksum: 314A53D4242BAF1B
Show »

FASTA1,466164,304
Isoform 5 (Delexon-17-18) [UniParc].

Checksum: 6CAB8926692A0377
Show »

FASTA1,416158,949
Isoform 6 (Delexon-17-30) [UniParc].

Checksum: E76D558115609C22
Show »

FASTA1,407157,683
Isoform 7 (Delexon-18-30) [UniParc].

Checksum: 6AAC80E7E87AD25D
Show »

FASTA1,410158,282
Isoform 8 (Delexon-17-18-30) [UniParc].

Checksum: B3FD697CE71EBB51
Show »

FASTA1,351151,661
Isoform 9 [UniParc].

Checksum: 5AE3F0E657F948F8
Show »

FASTA1,541172,640

References

« Hide 'large scale' references
[1]"Overexpression of a transporter gene in a multidrug-resistant human lung cancer cell line."
Cole S.P.C., Bhardwaj G., Gerlach J.H., Mackie J.E., Grant C.E., Almquist K.C., Stewart A.J., Kurz E.U., Duncan A.M.V., Deeley R.G.
Science 258:1650-1654(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-117.
[2]"Multidrug resistance-associated protein: sequence correction."
Cole S.P.C., Deeley R.G.
Science 260:879-879(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Analysis of the intron-exon organization of the human multidrug-resistance protein gene (MRP) and alternative splicing of its mRNA."
Grant C.E., Kurz E.U., Cole S.P.C., Deeley R.G.
Genomics 45:368-378(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANT THR-117.
[4]NIEHS SNPs program
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-671; GLN-723; THR-861; SER-1047 AND ILE-1146.
[5]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-1531 (ISOFORM 9).
Tissue: Brain.
[7]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 516-1531.
[8]"Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus."
Hipfner D.R., Almquist K.C., Leslie E.M., Gerlach J.H., Grant C.E., Deeley R.G., Cole S.P.C.
J. Biol. Chem. 272:23623-23630(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY, GLYCOSYLATION AT ASN-19; ASN-23 AND ASN-1006.
[9]"Topology mapping of the amino-terminal half of multidrug resistance-associated protein by epitope insertion and immunofluorescence."
Kast C., Gros P.
J. Biol. Chem. 272:26479-26487(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[10]"Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein."
Kast C., Gros P.
Biochemistry 37:2305-2313(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[11]"Characterization of a leukotriene C4 export mechanism in human platelets: possible involvement of multidrug resistance-associated protein 1."
Sjoelinder M., Tornhamre S., Claesson H.-E., Hydman J., Lindgren J.A.
J. Lipid Res. 40:439-446(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The leukotriene C(4) transporter MRP1 regulates CCL19 (MIP-3beta, ELC)-dependent mobilization of dendritic cells to lymph nodes."
Robbiani D.F., Finch R.A., Jaeger D., Muller W.A., Sartorelli A.C., Randolph G.J.
Cell 103:757-768(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation."
Cui L., Hou Y.-X., Riordan J.R., Chang X.-B.
Arch. Biochem. Biophys. 392:153-161(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-792; ASP-793; LYS-1333 AND 1454-ASP-GLU-1455.
[14]"Mutation of a single conserved tryptophan in multidrug resistance protein 1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of organic anion transport."
Ito K., Olsen S.L., Qiu W., Deeley R.G., Cole S.P.C.
J. Biol. Chem. 276:15616-15624(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-1246.
[15]"Identification of an amino acid residue in multidrug resistance protein 1 critical for conferring resistance to anthracyclines."
Zhang D.-W., Cole S.P.C., Deeley R.G.
J. Biol. Chem. 276:13231-13239(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-1089.
[16]"Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transporter."
Situ D., Haimeur A., Conseil G., Sparks K.E., Zhang D.-W., Deeley R.G., Cole S.P.C.
J. Biol. Chem. 279:38871-38880(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-1046; ASP-1084 AND ARG-1131.
[17]"Transmembrane helix 11 of multidrug resistance protein 1 (MRP1/ABCC1): identification of polar amino acids important for substrate specificity and binding of ATP at nucleotide binding domain 1."
Zhang D.-W., Nunoya K., Vasa M., Gu H.-M., Theis A., Cole S.P.C., Deeley R.G.
Biochemistry 43:9413-9425(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLN-580; THR-581; SER-585; ASN-597; SER-604 AND SER-605.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1)."
Conseil G., Deeley R.G., Cole S.P.
J. Biol. Chem. 281:43-50(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-1138; LYS-1141 AND ARG-1142, SUBCELLULAR LOCATION.
[20]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905 AND SER-930, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site."
Ramaen O., Leulliot N., Sizun C., Ulryck N., Pamlard O., Lallemand J.-Y., Tilbeurgh H., Jacquet E.
J. Mol. Biol. 359:940-949(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 642-871 IN COMPLEX WITH MG-ATP.
[27]"Mutations in a gene encoding an ABC transporter cause pseudoxanthoma elasticum."
Le Saux O., Urban Z., Tschuch C., Csiszar K., Bacchelli B., Quaglino D., Pasquali-Ronchetti I., Pope F.M., Richards A., Terry S., Bercovitch L., de Paepe A., Boyd C.D.
Nat. Genet. 25:223-227(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLN-633 AND VAL-671.
[28]"Pseudoxanthoma elasticum: mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter."
Ringpfeil F., Lebwohl M.G., Christiano A.M., Uitto J.
Proc. Natl. Acad. Sci. U.S.A. 97:6001-6006(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-671.
[29]"Identification of human multidrug resistance protein 1 (MRP1) mutations and characterization of a G671V substitution."
Conrad S., Kauffmann H.-M., Ito K., Deeley R.G., Cole S.P.C., Schrenk D.
J. Hum. Genet. 46:656-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-433, CHARACTERIZATION OF VARIANT VAL-671.
[30]"Identification of novel polymorphisms in the pM5 and MRP1 (ABCC1) genes at locus 16p13.1 and exclusion of both genes as responsible for pseudoxanthoma elasticum."
Perdu J., Germain D.P.
Hum. Mutat. 17:74-75(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-117 AND LEU-1512.
[31]"Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT, in healthy Japanese subjects."
Ito S., Ieiri I., Tanabe M., Suzuki A., Higuchi S., Otsubo K.
Pharmacogenetics 11:175-184(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-43; ILE-73; GLN-723 AND GLN-1058.
[32]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-433.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05628 mRNA. Translation: AAB46616.1.
AF022853 expand/collapse EMBL AC list , AF022827, AF022828, AF022829, AF022831, AF022833, AF022835, AF022837, AF022839, AF022841, AF022850, AF022849, AF022848, AF022847, AF022846, AF022845, AF022844, AF022843, AF022842, AF022852, AF022851, AF022840, AF022838, AF022836, AF022834, AF022832, AF022826, AF022825, AF022824, AF022830 Genomic DNA. Translation: AAB83979.1.
AF022853 expand/collapse EMBL AC list , AF022824, AF022825, AF022826, AF022828, AF022830, AF022832, AF022834, AF022836, AF022838, AF022848, AF022847, AF022846, AF022845, AF022844, AF022843, AF022842, AF022841, AF022839, AF022852, AF022851, AF022850, AF022849, AF022837, AF022835, AF022833, AF022831, AF022829, AF022827 Genomic DNA. Translation: AAB83980.1.
AF022853 expand/collapse EMBL AC list , AF022824, AF022825, AF022826, AF022827, AF022829, AF022831, AF022833, AF022835, AF022837, AF022847, AF022846, AF022845, AF022844, AF022843, AF022842, AF022841, AF022840, AF022838, AF022852, AF022851, AF022850, AF022849, AF022848, AF022836, AF022834, AF022832, AF022830, AF022828 Genomic DNA. Translation: AAB83981.1.
AF022853 expand/collapse EMBL AC list , AF022824, AF022825, AF022826, AF022827, AF022828, AF022829, AF022830, AF022831, AF022832, AF022833, AF022834, AF022835, AF022836, AF022837, AF022838, AF022839, AF022840, AF022841, AF022842, AF022843, AF022844, AF022845, AF022846, AF022847, AF022848, AF022849, AF022850, AF022851 Genomic DNA. Translation: AAB83983.1.
EF419769 Genomic DNA. Translation: ABN79590.1.
AC025778 Genomic DNA. No translation available.
AC130651 Genomic DNA. No translation available.
AC136624 Genomic DNA. No translation available.
AB209120 mRNA. Translation: BAD92357.1.
U91318 Genomic DNA. Translation: AAC15784.1.
AC003026 Genomic DNA. Translation: AAC05808.1.
PIRDVHUAR. A44231.
RefSeqNP_004987.2. NM_004996.3.
XP_005255386.1. XM_005255329.1.
UniGeneHs.391464.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CBZX-ray1.50A642-871[»]
ProteinModelPortalP33527.
SMRP33527. Positions 642-871.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110503. 30 interactions.
IntActP33527. 5 interactions.
MINTMINT-2802626.

Chemistry

ChEMBLCHEMBL3004.
DrugBankDB00694. Daunorubicin.
DB01016. Glibenclamide.
DB01032. Probenecid.
DB01232. Saquinavir.
DB01138. Sulfinpyrazone.

Protein family/group databases

TCDB3.A.1.208.8. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteP33527.

Polymorphism databases

DMDM296439301.

Proteomic databases

PaxDbP33527.
PRIDEP33527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345148; ENSP00000263014; ENSG00000103222. [P33527-4]
ENST00000346370; ENSP00000263019; ENSG00000103222. [P33527-3]
ENST00000349029; ENSP00000263016; ENSG00000103222. [P33527-5]
ENST00000351154; ENSP00000263017; ENSG00000103222. [P33527-2]
ENST00000399408; ENSP00000382340; ENSG00000103222. [P33527-9]
ENST00000399410; ENSP00000382342; ENSG00000103222. [P33527-1]
GeneID4363.
KEGGhsa:4363.
UCSCuc010bvi.3. human. [P33527-1]

Organism-specific databases

CTD4363.
GeneCardsGC16P016043.
H-InvDBHIX0134370.
HGNCHGNC:51. ABCC1.
HPACAB016097.
HPA002380.
MIM158343. gene.
neXtProtNX_P33527.
PharmGKBPA244.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1132.
HOVERGENHBG108314.
KOK05665.
OMADISRHHN.
OrthoDBEOG7MWGW0.
PhylomeDBP33527.
TreeFamTF105199.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP33527.
BgeeP33527.
CleanExHS_ABCC1.
GenevestigatorP33527.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR005292. Multidrug-R_assoc.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 2 hits.
TIGRFAMsTIGR00957. MRP_assoc_pro. 1 hit.
PROSITEPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABCC1. human.
EvolutionaryTraceP33527.
GeneWikiABCC1.
GenomeRNAi4363.
NextBio17171.
PROP33527.
SOURCESearch...

Entry information

Entry nameMRP1_HUMAN
AccessionPrimary (citable) accession number: P33527
Secondary accession number(s): A3RJX2 expand/collapse secondary AC list , C9JPJ4, O14819, O43333, P78419, Q59GI9, Q9UQ97, Q9UQ99, Q9UQA0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM