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Reviewed, UniProtKB/Swiss-Prot P08183 (MDR1_HUMAN)

Last modified October 13, 2009. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Multidrug resistance protein 1
    EC=3.6.3.44
Alternative name(s):
    ATP-binding cassette sub-family B member 1
    P-glycoprotein 1
    CD_antigen=CD243
Gene names
Name: ABCB1
Synonyms: MDR1, PGY1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1280 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.

Catalytic activity

ATP + H2O + xenobiotic(In) = ADP + phosphate + xenobiotic(Out).

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in liver, kidney, small intestine and brain.

Polymorphism

Genetic variation in ABCB1 may play a role in patients who do not respond to drug treatment.

Involvement in disease

Genetic variations in ABCB1 are associated with susceptibility to inflammatory bowel disease type 13 (IBD13) [MIM:612244]. Inflammatory bowel disease is characterized by a chronic relapsing intestinal inflammation. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may involve any part of the gastrointestinal tract, but most frequently the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. Crohn disease and ulcerative colitis are commonly classified as autoimmune diseases. Ref.18

Sequence similarities

Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. [View classification]

Contains 2 ABC transmembrane type-1 domains.

Contains 2 ABC transporter domains.

Sequence caution

The sequence AAB69423.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Transmembrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processresponse to drug

Traceable author statement. Source: ProtInc

transport

Traceable author statement. Source: ProtInc

   Cellular componentcell surface

Inferred from direct assay. Source: UniProtKB

focal adhesion

Inferred from direct assay. Source: HPA

integral to membrane

Traceable author statement. Source: ProtInc

membrane fraction

Traceable author statement. Source: ProtInc

nucleus

Inferred from direct assay. Source: HPA

   Molecular functionATP binding

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: IntAct

xenobiotic-transporting ATPase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RNF2Q994961EBI-1057359,EBI-722416

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12801280Multidrug resistance protein 1
PRO_0000093332

Regions

Topological domain1 – 5151Cytoplasmic Potential
Transmembrane52 – 7221 Potential
Transmembrane120 – 14021 Potential
Transmembrane189 – 20921 Potential
Transmembrane216 – 23621 Potential
Transmembrane297 – 31721 Potential
Transmembrane326 – 34621 Potential
Topological domain347 – 710364Cytoplasmic Potential
Transmembrane711 – 73121 Potential
Transmembrane757 – 77721 Potential
Transmembrane833 – 85321 Potential
Transmembrane854 – 87421 Potential
Transmembrane937 – 95721 Potential
Transmembrane974 – 99421 Potential
Topological domain995 – 1280286Cytoplasmic Potential
Domain51 – 357307ABC transmembrane type-1 1
Domain392 – 628237ABC transporter 1
Domain711 – 1000290ABC transmembrane type-1 2
Domain1035 – 1273239ABC transporter 2
Nucleotide binding427 – 4348ATP 1 By similarity
Nucleotide binding1070 – 10778ATP 2 By similarity

Amino acid modifications

Modified residue6601Phosphoserine By similarity
Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential

Natural variations

Natural variant171F → L: dbSNP rs28381804. Ref.4
VAR_022276
Natural variant211N → D: dbSNP rs9282564. Ref.4 Ref.5 Ref.12 Ref.13 Ref.14
VAR_014704
Natural variant441N → S: dbSNP rs1202183.
VAR_055423
Natural variant801A → E: dbSNP rs9282565.
VAR_055424
Natural variant1031F → L Rare polymorphism. Ref.13
VAR_015001
Natural variant1081E → K
VAR_018351
Natural variant1851G → V in a colchicine-selected multidrug-resistant cell line; confers increased resistance to colchicine. dbSNP rs1128501. Ref.1 Ref.3 Ref.10
VAR_015002
Natural variant2611I → V: dbSNP rs36008564.
VAR_055425
Natural variant4001S → N: dbSNP rs2229109. Ref.4 Ref.13 Ref.14
VAR_015003
Natural variant5661E → K: dbSNP rs28381902. Ref.4
VAR_022277
Natural variant5931R → C: dbSNP rs28381914. Ref.4
VAR_022278
Natural variant5991A → T: dbSNP rs2235036.
VAR_055426
Natural variant6691R → C: dbSNP rs35023033.
VAR_055427
Natural variant8011V → M: dbSNP rs2235039.
VAR_055428
Natural variant8291I → V: dbSNP rs2032581.
VAR_055429
Natural variant8361I → V: dbSNP rs28381967. Ref.4
VAR_022279
Natural variant8871K → N in a colorectal cancer sample; somatic mutation. Ref.20
VAR_035737
Natural variant8931S → A Common allele; associated with susceptibility to IBD13; has decreased enzyme activity. dbSNP rs2032582. Ref.18 Ref.4 Ref.14 Ref.1 Ref.3 Ref.2 Ref.11 Ref.17
VAR_013361
Natural variant8931S → T Rare allele. dbSNP rs2032582. Ref.18 Ref.14 Ref.17
VAR_013362
Natural variant9861M → V
VAR_018352
Natural variant9991A → T
VAR_015004
Natural variant10511P → A: dbSNP rs28401798. Ref.4
VAR_022280
Natural variant11071Q → P: dbSNP rs55852620. Ref.14
VAR_015005
Natural variant11411S → T: dbSNP rs2229107. Ref.4
VAR_022281
Natural variant12511V → I
VAR_018353

Experimental info

Sequence conflict231S → R in CAA41558. Ref.8
Sequence conflict3361Missing in AAB69423. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P08183-1 [UniParc].

Last modified May 26, 2009. Version 3.
Checksum: F0230744AB288C73

FASTA1,280141,479
        10         20         30         40         50         60 
MDLEGDRNGG AKKKNFFKLN NKSEKDKKEK KPTVSVFSMF RYSNWLDKLY MVVGTLAAII 

        70         80         90        100        110        120 
HGAGLPLMML VFGEMTDIFA NAGNLEDLMS NITNRSDIND TGFFMNLEED MTRYAYYYSG 

       130        140        150        160        170        180 
IGAGVLVAAY IQVSFWCLAA GRQIHKIRKQ FFHAIMRQEI GWFDVHDVGE LNTRLTDDVS 

       190        200        210        220        230        240 
KINEGIGDKI GMFFQSMATF FTGFIVGFTR GWKLTLVILA ISPVLGLSAA VWAKILSSFT 

       250        260        270        280        290        300 
DKELLAYAKA GAVAEEVLAA IRTVIAFGGQ KKELERYNKN LEEAKRIGIK KAITANISIG 

       310        320        330        340        350        360 
AAFLLIYASY ALAFWYGTTL VLSGEYSIGQ VLTVFFSVLI GAFSVGQASP SIEAFANARG 

       370        380        390        400        410        420 
AAYEIFKIID NKPSIDSYSK SGHKPDNIKG NLEFRNVHFS YPSRKEVKIL KGLNLKVQSG 

       430        440        450        460        470        480 
QTVALVGNSG CGKSTTVQLM QRLYDPTEGM VSVDGQDIRT INVRFLREII GVVSQEPVLF 

       490        500        510        520        530        540 
ATTIAENIRY GRENVTMDEI EKAVKEANAY DFIMKLPHKF DTLVGERGAQ LSGGQKQRIA 

       550        560        570        580        590        600 
IARALVRNPK ILLLDEATSA LDTESEAVVQ VALDKARKGR TTIVIAHRLS TVRNADVIAG 

       610        620        630        640        650        660 
FDDGVIVEKG NHDELMKEKG IYFKLVTMQT AGNEVELENA ADESKSEIDA LEMSSNDSRS 

       670        680        690        700        710        720 
SLIRKRSTRR SVRGSQAQDR KLSTKEALDE SIPPVSFWRI MKLNLTEWPY FVVGVFCAII 

       730        740        750        760        770        780 
NGGLQPAFAI IFSKIIGVFT RIDDPETKRQ NSNLFSLLFL ALGIISFITF FLQGFTFGKA 

       790        800        810        820        830        840 
GEILTKRLRY MVFRSMLRQD VSWFDDPKNT TGALTTRLAN DAAQVKGAIG SRLAVITQNI 

       850        860        870        880        890        900 
ANLGTGIIIS FIYGWQLTLL LLAIVPIIAI AGVVEMKMLS GQALKDKKEL EGSGKIATEA 

       910        920        930        940        950        960 
IENFRTVVSL TQEQKFEHMY AQSLQVPYRN SLRKAHIFGI TFSFTQAMMY FSYAGCFRFG 

       970        980        990       1000       1010       1020 
AYLVAHKLMS FEDVLLVFSA VVFGAMAVGQ VSSFAPDYAK AKISAAHIIM IIEKTPLIDS 

      1030       1040       1050       1060       1070       1080 
YSTEGLMPNT LEGNVTFGEV VFNYPTRPDI PVLQGLSLEV KKGQTLALVG SSGCGKSTVV 

      1090       1100       1110       1120       1130       1140 
QLLERFYDPL AGKVLLDGKE IKRLNVQWLR AHLGIVSQEP ILFDCSIAEN IAYGDNSRVV 

      1150       1160       1170       1180       1190       1200 
SQEEIVRAAK EANIHAFIES LPNKYSTKVG DKGTQLSGGQ KQRIAIARAL VRQPHILLLD 

      1210       1220       1230       1240       1250       1260 
EATSALDTES EKVVQEALDK AREGRTCIVI AHRLSTIQNA DLIVVFQNGR VKEHGTHQQL 

      1270       1280 
LAQKGIYFSM VSVQAGTKRQ 

« Hide

References

« Hide 'large scale' references
[1]"Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells."
Chen C.-J., Chin J.E., Ueda K., Clark D.P., Pastan I., Gottesman M.M., Roninson I.B.
Cell 47:381-389(1986) [PubMed: 2876781] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-185 AND ALA-893.
[2]"Genomic organization of the human multidrug resistance (MDR1) gene and origin of P-glycoproteins."
Chen C.-J., Clark D.P., Ueda K., Pastan I., Gottesman M.M., Roninson I.B.
J. Biol. Chem. 265:506-514(1990) [PubMed: 1967175] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-893.
[3]"Multidrug-resistant human sarcoma cells with a mutant P-glycoprotein, altered phenotype, and resistance to cyclosporins."
Chen G., Duran G.E., Steger K.A., Lacayo N.J., Jaffrezou J.P., Dumontet C., Sikic B.I.
J. Biol. Chem. 272:5974-5982(1997) [PubMed: 9038218] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-185 AND ALA-893.
[4]NIEHS SNPs program
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-17; ASP-21; ASN-400; LYS-566; CYS-593; VAL-836; ALA-893; ALA-1051; THR-1141 AND ILE-1251.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-21.
Tissue: Thalamus.
[6]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"mdr1/P-glycoprotein gene segments analyzed from various human leukemic cell lines exhibiting different multidrug resistance profiles."
Gekeler V., Weger S., Probst H.
Biochem. Biophys. Res. Commun. 169:796-802(1990) [PubMed: 1972623] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-215 AND 800-856.
[8]"P-glycoprotein gene (MDR1) cDNA from human adrenal: normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance."
Kioka N., Tsubota J., Kakehi Y., Komano T., Gottesman M.M., Pastan I., Ueda K.
Biochem. Biophys. Res. Commun. 162:224-231(1989) [PubMed: 2568832] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-23.
[9]"ABC drug transporters: hereditary polymorphisms and pharmacological impact in MDR1, MRP1 and MRP2."
Kerb R., Hoffmeyer S., Brinkmann U.
Pharmacogenomics 2:51-64(2001) [PubMed: 11258197] [Abstract]
Cited for: REVIEW.
[10]"An altered pattern of cross-resistance in multidrug-resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene."
Choi K.H., Chen C.-J., Kriegler M., Roninson I.B.
Cell 53:519-529(1988) [PubMed: 2897240] [Abstract]
Cited for: VARIANT VAL-185.
[11]"Genetic polymorphism in MDR-1: a tool for examining allelic expression in normal cells, unselected and drug-selected cell lines, and human tumors."
Mickley L.A., Lee J.-S., Weng Z., Zhan Z., Alvarez M., Wilson W., Bates S.E., Fojo T.
Blood 91:1749-1756(1998) [PubMed: 9473242] [Abstract]
Cited for: VARIANTS ALA-893 AND THR-999.
[12]"A new polymorphism (N21D) in the exon 2 of the human MDR1 gene encoding the P-glycoprotein."
Decleves X., Chevillard S., Charpentier C., Vielh P., Laplanche J.-L.
Hum. Mutat. 15:486-486(2000) [PubMed: 10790226] [Abstract]
Cited for: VARIANT ASP-21.
[13]"Functional polymorphisms of the human multidrug-resistance gene: multiple sequence variations and correlation of one allele with P-glycoprotein expression and activity in vivo."
Hoffmeyer S., Burk O., von Richter O., Arnold H.P., Brockmoeller J., Johne A., Cascorbi I., Gerloff T., Roots I., Eichelbaum M., Brinkmann U.
Proc. Natl. Acad. Sci. U.S.A. 97:3473-3478(2000) [PubMed: 10716719] [Abstract]
Cited for: VARIANTS ASP-21; LEU-103 AND ASN-400.
[14]"Frequency of single nucleotide polymorphisms in the P-glycoprotein drug transporter MDR1 gene in white subjects."
Cascorbi I., Gerloff T., Johne A., Meisel C., Hoffmeyer S., Schwab M., Schaeffeler E., Eichelbaum M., Brinkmann U., Roots I.
Clin. Pharmacol. Ther. 69:169-174(2001) [PubMed: 11240981] [Abstract]
Cited for: VARIANTS ASP-21; ASN-400; ALA-893; THR-893 AND PRO-1107.
[15]"Polymorphism of MDR1 gene in healthy Japanese subjects: a novel SNP with an amino acid substitution (Glu108Lys)."
Honda T., Dan Y., Koyabu N., Ieiri I., Otsubo K., Higuchi S., Ohtani H., Sawada J.
Drug Metab. Pharmacokinet. 17:479-481(2002) [PubMed: 15618700] [Abstract]
Cited for: VARIANT LYS-108.
[16]"Twelve novel single nucleotide polymorphisms in ABCB1/MDR1 among Japanese patients with ventricular tachycardia who were administered amiodarone."
Itoda M., Saito Y., Komamura K., Ueno K., Kamakura S., Ozawa S., Sawada J.
Drug Metab. Pharmacokinet. 17:566-571(2002) [PubMed: 15618713] [Abstract]
Cited for: VARIANT ILE-1251.
[17]"Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population."
Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., Higuchi S., Nakamura Y.
J. Hum. Genet. 47:38-50(2002) [PubMed: 11829140] [Abstract]
Cited for: VARIANTS ALA-893 AND THR-893.
[18]"MDR1 Ala893 polymorphism is associated with inflammatory bowel disease."
Brant S.R., Panhuysen C.I.M., Nicolae D., Reddy D.M., Bonen D.K., Karaliukas R., Zhang L., Swanson E., Datta L.W., Moran T., Ravenhill G., Duerr R.H., Achkar J.-P., Karban A.S., Cho J.H.
Am. J. Hum. Genet. 73:1282-1292(2003) [PubMed: 14610718] [Abstract]
Cited for: VARIANTS ALA-893 AND THR-893, ASSOCIATION WITH SUSCEPTIBILITY TO IBD13.
[19]Erratum
Brant S.R., Panhuysen C.I.M., Nicolae D., Reddy D.M., Bonen D.K., Karaliukas R., Zhang L., Swanson E., Datta L.W., Moran T., Ravenhill G., Duerr R.H., Achkar J.-P., Karban A.S., Cho J.H.
Am. J. Hum. Genet. 74:1080-1080(2004)
[20]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-887.
+Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

P-glycoprotein entry

Cross-references

Sequence databases

M14758 mRNA. Translation: AAA59575.1.
M29447 expand/collapse EMBL AC list , M29424, M29425, M29426, M29427, M29428, M29429, M29430, M29431, M29432, M29433, M29434, M29435, M29436, M29437, M29438, M29439, M29440, M29441, M29442, M29443, M29444, M29445, M29446 Genomic DNA. Translation: AAA59576.1.
AF016535 mRNA. Translation: AAB69423.1.
AY910577 Genomic DNA. Translation: AAW82430.1.
AK290159 mRNA. Translation: BAF82848.1.
AC002457 Genomic DNA. Translation: AAM49149.1. Sequence problems.
AC005068 Genomic DNA. No translation available.
M37724 Genomic DNA. Translation: AAA88047.1.
M37725 Genomic DNA. Translation: AAA88048.1.
X58723 Genomic DNA. Translation: CAA41558.1.
IPIIPI00027481.
PIRDVHU1. A34914.
RefSeqNP_000918.2.
UniGeneHs.489033

3D structure databases

HSSPHSSP built from PDB template 1MT0 based on UniProtKB P08716.
ModBaseSearch...

Protein-protein interaction databases

IntActP08183. 2 interactions.
STRINGP08183.

Protein family/group databases

TCDB3.A.1.201.1. ATP-binding cassette (ABC) superfamily.

PTM databases

PhosphoSiteP08183.

Proteomic databases

PRIDEP08183.

Genome annotation databases

EnsemblENST00000265724; ENSP00000265724; ENSG00000085563; Homo sapiens. [Genome view]
ENST00000394661; ENSP00000378156; ENSG00000085563; Homo sapiens. [Genome view]
ENST00000415096; ENSP00000411075; ENSG00000085563; Homo sapiens. [Genome view]
ENST00000416177; ENSP00000399419; ENSG00000085563; Homo sapiens. [Genome view]
GeneID5243.
KEGGhsa:5243.

Organism-specific databases

CTD5243.
GeneCardsGC07M086970.
H-InvDBHIX0033521.
HIX0033618.
HGNCHGNC:40. ABCB1.
HPACAB001716.
HPA002199.
MIM120080. phenotype.
171050. gene.
612244. phenotype.
PharmGKBPA267.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP08183.
HOVERGENP08183.

Enzyme and pathway databases

BRENDA3.6.3.44. 247.
Pathway_Interaction_DBhif1_tfpathway. HIF-1-alpha transcription factor network.

Gene expression databases

ArrayExpressP08183.
BgeeP08183.
CleanExHS_ABCB1.
GenevestigatorP08183.
GermOnlineENSG00000085563. Homo sapiens.

Family and domain databases

InterProIPR001140. ABC_TM_transpt.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR017940. ABC_transporter_type1.
IPR003593. ATPase_AAA+_core.
[Graphical view]
PfamPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
ProDomPD000006. ABC_transporter. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
PROSITEPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00171. Adenosine triphosphate.
DB00802. Alfentanil.
DB01169. Arsenic trioxide.
DB01072. Atazanavir.
DB01136. Carvedilol.
DB01394. Colchicine.
DB00091. Cyclosporine.
DB00694. Daunorubicin.
DB00975. Dipyridamole.
DB01196. Estramustine.
DB00875. Flupenthixol.
DB00619. Imatinib.
DB01167. Itraconazole.
DB00622. Nicardipine.
DB01182. Propafenone.
DB01103. Quinacrine.
DB00908. Quinidine.
DB00243. Ranolazine.
DB01045. Rifampin.
DB00778. Roxithromycin.
DB01232. Saquinavir.
DB00675. Tamoxifen.
DB00570. Vinblastine.
NextBio20254.
SOURCESearch...

Entry information

Entry nameMDR1_HUMAN
AccessionPrimary (citable) accession number: P08183
Secondary accession number(s): A8K294, Q12755, Q14812
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 26, 2009
Last modified: October 13, 2009
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents