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Mucin-1 (MUC-1) (Breast carcinoma-associated antigen DF3) (Cancer antigen 15-3) (CA 15-3) (Carcinoma-associated mucin) (Episialin) (H23AG) (Krebs von den Lungen-6) (KL-6) (PEMT) (Peanut-reactive urinary mucin) (PUM) (Polymorphic epithelial mucin) (PEM) (Tumor-associated epithelial membrane antigen) (EMA) (Tumor-associated mucin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]

 MUC1_HUMAN              Reviewed;        1255 AA.
P15941; A5YRV1; A6ZID9; A6ZIE0; B1AVQ8; B1AVR0; B6ECA1; E7ESE5; E7EUG9;
P13931; P15942; P17626; Q0VAP5; Q0VAP6; Q14128; Q14876; Q16437; Q16442;
Q16615; Q6S4Y3; Q7Z547; Q7Z548; Q7Z550; Q7Z552; Q9BXA4; Q9UE75; Q9UE76;
Q9UQL1; Q9Y4J2;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
07-APR-2021, entry version 227.
RecName: Full=Mucin-1;
Short=MUC-1;
AltName: Full=Breast carcinoma-associated antigen DF3;
AltName: Full=Cancer antigen 15-3;
Short=CA 15-3;
AltName: Full=Carcinoma-associated mucin;
AltName: Full=Episialin;
AltName: Full=H23AG;
AltName: Full=Krebs von den Lungen-6;
Short=KL-6;
AltName: Full=PEMT;
AltName: Full=Peanut-reactive urinary mucin;
Short=PUM;
AltName: Full=Polymorphic epithelial mucin;
Short=PEM;
AltName: Full=Tumor-associated epithelial membrane antigen;
Short=EMA;
AltName: Full=Tumor-associated mucin;
AltName: CD_antigen=CD227;
Contains:
RecName: Full=Mucin-1 subunit alpha;
Short=MUC1-NT;
Short=MUC1-alpha;
Contains:
RecName: Full=Mucin-1 subunit beta;
Short=MUC1-beta;
AltName: Full=MUC1-CT;
Flags: Precursor;
Name=MUC1; Synonyms=PUM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Pancreatic carcinoma;
PubMed=2394722;
Lan M.S., Batra S.K., Qi W.-N., Metzgar R.S., Hollingsworth M.A.;
"Cloning and sequencing of a human pancreatic tumor mucin cDNA.";
J. Biol. Chem. 265:15294-15299(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=2318825;
Ligtenberg M.J.L., Vos H.L., Gennissen A.M.C., Hilkens J.;
"Episialin, a carcinoma-associated mucin, is generated by a polymorphic
gene encoding splice variants with alternative amino termini.";
J. Biol. Chem. 265:5573-5578(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary carcinoma;
PubMed=1697589;
Gendler S.J., Lancaster C.A., Taylor-Papadimitriou J., Duhig T., Peat N.,
Burchell J., Pemberton L., Lalani E.-N., Wilson D.;
"Molecular cloning and expression of human tumor-associated polymorphic
epithelial mucin.";
J. Biol. Chem. 265:15286-15293(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=2268309; DOI=10.1016/s0006-291x(05)80888-5;
Lancaster C.A., Peat N., Duhig T., Wilson D., Taylor-Papadimitriou J.,
Gendler S.J.;
"Structure and expression of the human polymorphic epithelial mucin gene:
an expressed VNTR unit.";
Biochem. Biophys. Res. Commun. 173:1019-1029(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Mammary carcinoma;
PubMed=2351132; DOI=10.1111/j.1432-1033.1990.tb15511.x;
Wreschner D.H., Hareuveni M., Tsarfaty I., Smorodinsky N., Horev J.,
Zaretsky J., Kotkes P., Weiss M., Lathe R., Dion A., Keydar I.;
"Human epithelial tumor antigen cDNA sequences. Differential splicing may
generate multiple protein forms.";
Eur. J. Biochem. 189:463-473(1990).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary carcinoma;
PubMed=2112460; DOI=10.1111/j.1432-1033.1990.tb15512.x;
Hareuveni M., Tsarfaty I., Zaretsky J., Kotkes P., Horev J., Zrihan S.,
Weiss M., Green S., Lathe R., Keydar I., Wreschner D.H.;
"A transcribed gene, containing a variable number of tandem repeats, codes
for a human epithelial tumor antigen. cDNA cloning, expression of the
transfected gene and over-expression in breast cancer tissue.";
Eur. J. Biochem. 189:475-486(1990).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=1688329; DOI=10.1016/0378-1119(90)90242-j;
Tsarfaty I., Hareuveni M., Horev J., Zaretsky J., Weiss M., Jeltsch J.-M.,
Garnier J.-M., Lathe R., Keydar I., Wreschner D.H.;
"Isolation and characterization of an expressed hypervariable gene coding
for a breast-cancer-associated antigen.";
Gene 93:313-318(1990).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM Y).
PubMed=7925397; DOI=10.1111/j.1432-1033.1994.00787.x;
Zrihan-Licht S., Vos H.L., Baruch A., Elroy-Stein O., Sagiv D., Keydar I.,
Hilkens J., Wreschner D.H.;
"Characterization and molecular cloning of a novel MUC1 protein, devoid of
tandem repeats, expressed in human breast cancer tissue.";
Eur. J. Biochem. 224:787-795(1994).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; Y AND 8), AND TISSUE SPECIFICITY.
PubMed=9212228;
DOI=10.1002/(sici)1097-0215(19970703)72:1<87::aid-ijc13>3.0.co;2-7;
Oosterkamp H.M., Scheiner L., Stefanova M.C., Lloyd K.O., Finstad C.L.;
"Comparison of MUC-1 mucin expression in epithelial and non-epithelial
cancer cell lines and demonstration of a new short variant form (MUC-
1/Z).";
Int. J. Cancer 72:87-94(1997).
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZD).
PubMed=15623537; DOI=10.1074/jbc.m406943200;
Levitin F., Baruch A., Weiss M., Stiegman K., Hartmann M.L.,
Yoeli-Lerner M., Ziv R., Zrihan-Licht S., Shina S., Gat A., Lifschitz B.,
Simha M., Stadler Y., Cholostoy A., Gil B., Greaves D., Keydar I.,
Zaretsky J., Smorodinsky N., Wreschner D.H.;
"A novel protein derived from the MUC1 gene by alternative splicing and
frameshifting.";
J. Biol. Chem. 280:10655-10663(2005).
[11]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; E2; J13; M6; S2; T10; Y-LSP AND
ZD), ALTERNATIVE SPLICING, AND VARIANT MET-1117.
PubMed=22941036; DOI=10.1007/s00262-012-1325-2;
Zhang L., Vlad A., Milcarek C., Finn O.J.;
"Human mucin MUC1 RNA undergoes different types of alternative splicing
resulting in multiple isoforms.";
Cancer Immunol. Immunother. 62:423-435(2013).
[12]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
TISSUE=Carcinoma;
Zhang L.X., Li C.H., Sun L.Y., Yue W.;
"Cloning of a new potential secreted short variant form of MUC1 mucin in
epithelial cancer cell line.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM Y), AND VARIANT MET-1117.
TISSUE=Cervix carcinoma;
PubMed=15969018;
Zhang L.X., Li C.H., Sun L.Y., Wang M., Lu H.J.;
"Soluble expression of peptide containing MUC1/Y-specific epitope in
Escherichia coli and preparation of the antibody.";
Sheng Wu Gong Cheng Xue Bao 19:337-342(2003).
[14]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F).
Zhang L.X., Lu H.J.;
"Cloning of a new MUC1 short variant mRNA F from HeLa cells.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S2).
Zhang L.X., Lu H.J.;
"Cloning of a new MUC1 short variant mRNA S2 from HeLa cells.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M6).
Zhang L., Finn O.J.;
"Isolation of MUC1 isoforms from MCF7 cells.";
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-1117 AND ASN-1142.
NIEHS SNPs program;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[18]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[19]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[20]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS Y AND Y-LSP).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[21]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3417635;
Gendler S.J., Taylor-Papadimitriou J., Duhig T., Rothbard J., Burchell J.;
"A highly immunogenic region of a human polymorphic epithelial mucin
expressed by carcinomas is made up of tandem repeats.";
J. Biol. Chem. 263:12820-12823(1988).
[22]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-160 (ISOFORM 2).
PubMed=2597151; DOI=10.1016/s0006-291x(89)80014-2;
Abe M., Siddiqui J., Kufe D.;
"Sequence analysis of the 5' region of the human DF3 breast carcinoma-
associated antigen gene.";
Biochem. Biophys. Res. Commun. 165:644-649(1989).
[23]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-109 (ISOFORM 2).
TISSUE=Thyroid;
PubMed=8608966;
DOI=10.1002/(sici)1097-0215(19960328)66:1<55::aid-ijc10>3.0.co;2-a;
Weiss M., Baruch A., Keydar I., Wreschner D.H.;
"Preoperative diagnosis of thyroid papillary carcinoma by reverse
transcriptase polymerase chain reaction of the MUC1 gene.";
Int. J. Cancer 66:55-59(1996).
[24]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-89.
TISSUE=Lung;
PubMed=8604237; DOI=10.1159/000227547;
Yu C.J., Yang P.C., Shew J.Y., Hong T.M., Yang S.C., Lee Y.C., Lee L.N.,
Luh K.T., Wu C.W.;
"Mucin mRNA expression in lung adenocarcinoma cell lines and tissues.";
Oncology 53:118-126(1996).
[25]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-46 (ISOFORMS 3 AND 4).
TISSUE=Mammary carcinoma;
Buluwela L., Liu Q., Luqmani Y.A., Gomm J.J., Coombes R.C.;
Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
[26]
PROTEIN SEQUENCE OF 24-33; 28-37 AND 1098-1107, AND PROTEOLYTIC PROCESSING.
PubMed=11341784; DOI=10.1006/bbrc.2001.4775;
Parry S., Silverman H.S., McDermott K., Willis A., Hollingsworth M.A.,
Harris A.;
"Identification of MUC1 proteolytic cleavage sites in vivo.";
Biochem. Biophys. Res. Commun. 283:715-720(2001).
[27]
PROTEIN SEQUENCE OF 1098-1111, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
SER-1098.
PubMed=15987679; DOI=10.1074/jbc.m506047200;
Levitin F., Stern O., Weiss M., Gil-Henn C., Ziv R., Prokocimer Z.,
Smorodinsky N.I., Rubinstein D.B., Wreschner D.H.;
"The MUC1 SEA module is a self-cleaving domain.";
J. Biol. Chem. 280:33374-33386(2005).
[28]
PROTEIN SEQUENCE OF TANDEM REPEAT, IDENTIFICATION BY MASS SPECTROMETRY, AND
GLYCOSYLATION.
PubMed=10373415; DOI=10.1074/jbc.274.26.18165;
Mueller S., Alving K., Peter-Katalinic J., Zachara N., Gooley A.A.,
Hanisch F.-G.;
"High density O-glycosylation on tandem repeat peptide from secretory MUC1
of T47D breast cancer cells.";
J. Biol. Chem. 274:18165-18172(1999).
[29]
PHOSPHORYLATION.
PubMed=7988707; DOI=10.1016/0014-5793(94)01251-2;
Zrihan-Licht S., Baruch A., Elroy-Stein O., Keydar I., Wreschner D.H.;
"Tyrosine phosphorylation of the MUC1 breast cancer membrane proteins.
Cytokine receptor-like molecules.";
FEBS Lett. 356:130-136(1994).
[30]
IDENTIFICATION IN A COMPLEX WITH SOS1 AND GRB2, INTERACTION WITH GRB2 AND
SOS1, AND PHOSPHORYLATION.
PubMed=7664271;
Pandey P., Kharbanda S., Kufe D.;
"Association of the DF3/MUC1 breast cancer antigen with Grb2 and the
Sos/Ras exchange protein.";
Cancer Res. 55:4000-4003(1995).
[31]
GLYCOSYLATION AT THR-131 AND THR-139, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=7744025; DOI=10.1111/j.1432-1033.1995.0140l.x;
Stadie T.R., Chai W., Lawson A.M., Byfield P.G., Hanisch F.G.;
"Studies on the order and site specificity of GalNAc transfer to MUC1
tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase
from milk or mammary carcinoma cells.";
Eur. J. Biochem. 229:140-147(1995).
[32]
INTERACTION WITH CTNNB1 AND JUP, AND FUNCTION.
PubMed=9139698; DOI=10.1074/jbc.272.19.12492;
Yamamoto M., Bharti A., Li Y., Kufe D.;
"Interaction of the DF3/MUC1 breast carcinoma-associated antigen and beta-
catenin in cell adhesion.";
J. Biol. Chem. 272:12492-12494(1997).
[33]
GLYCOSYLATION.
PubMed=9312074; DOI=10.1074/jbc.272.40.24780;
Mueller S., Goletz S., Packer N.H., Gooley A.A., Lawson A.M.,
Hanisch F.-G.;
"Localization of O-glycosylation sites on glycopeptide fragments from
lactation-associated MUC1. All putative sites within the tandem repeat are
glycosylation targets in vivo.";
J. Biol. Chem. 272:24780-24793(1997).
[34]
DEVELOPMENTAL STAGE.
PubMed=9536947; DOI=10.1136/gut.42.2.220;
Reid C.J., Harris A.;
"Developmental expression of mucin genes in the human gastrointestinal
system.";
Gut 42:220-226(1998).
[35]
GLYCOSYLATION AT THR-131 AND THR-139, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=9597769;
DOI=10.1002/(sici)1096-9888(199804)33:4<358::aid-jms642>3.0.co;2-3;
Hanisch F.G., Green B.N., Bateman R., Peter-Katalinic J.;
"Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI
mass spectrometry.";
J. Mass Spectrom. 33:358-362(1998).
[36]
INTERACTION WITH GSK3B AND CTNNB1, PHOSPHORYLATION AT SER-1227, AND
MUTAGENESIS OF SER-1223 AND SER-1227.
PubMed=9819408; DOI=10.1128/mcb.18.12.7216;
Li Y., Bharti A., Chen D., Gong J., Kufe D.;
"Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-
associated antigen and beta-catenin.";
Mol. Cell. Biol. 18:7216-7224(1998).
[37]
CHARACTERIZATION (ISOFORM Y), AND MUTAGENESIS OF ASP-1116.
PubMed=10197628;
Baruch A., Hartmann M.-L., Yoeli M., Adereth Y., Greenstein S., Stadler Y.,
Skornik Y., Zaretsky J., Smorodinsky N.I., Keydar I., Wreschner D.H.;
"The breast cancer-associated MUC1 gene generates both a receptor and its
cognate binding protein.";
Cancer Res. 59:1552-1561(1999).
[38]
INTERACTION WITH ICAM1.
PubMed=11173916; DOI=10.1159/000051917;
Hayashi T., Takahashi T., Motoya S., Ishida T., Itoh F., Adachi M.,
Hinoda Y., Imai K.;
"MUC1 mucin core protein binds to the domain 1 of ICAM-1.";
Digestion 63 Suppl. 1:87-92(2001).
[39]
SUBCELLULAR LOCATION.
PubMed=11118479; DOI=10.1177/002215540104900107;
Bennett R. Jr., Jaervelae T., Engelhardt P., Kostamovaara L., Sparks P.,
Carpen O., Turunen O., Vaheri A.;
"Mucin MUC1 is seen in cell surface protrusions together with ezrin in
immunoelectron tomography and is concentrated at tips of filopodial
protrusions in MCF-7 breast carcinoma cells.";
J. Histochem. Cytochem. 49:67-77(2001).
[40]
INTERACTION WITH SRC; GSK3B AND CTNNB1, PHOSPHORYLATION AT TYR-1229, AND
MUTAGENESIS OF TYR-1229.
PubMed=11152665; DOI=10.1074/jbc.c000754200;
Li Y., Kuwahara H., Ren J., Wen G., Kufe D.;
"The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1
carcinoma-associated antigen with GSK3 beta and beta-catenin.";
J. Biol. Chem. 276:6061-6064(2001).
[41]
POLYMORPHISM WITHIN THE REPEAT.
PubMed=11350974; DOI=10.1074/jbc.m103187200;
Engelmann K., Baldus S.E., Hanisch F.-G.;
"Identification and topology of variant sequences within individual repeat
domains of the human epithelial tumor mucin MUC1.";
J. Biol. Chem. 276:27764-27769(2001).
[42]
INTERACTION WITH EGFR, PHOSPHORYLATION AT TYR-1229 BY EGFR, AND MUTAGENESIS
OF TYR-1191; TYR-1203; TYR-1209; TYR-1218 AND TYR-1229.
PubMed=11483589; DOI=10.1074/jbc.c100359200;
Li Y., Ren J., Yu W., Li Q., Kuwahara H., Yin L., Carraway K.L. III,
Kufe D.;
"The epidermal growth factor receptor regulates interaction of the human
DF3/MUC1 carcinoma antigen with c-Src and beta-catenin.";
J. Biol. Chem. 276:35239-35242(2001).
[43]
PHOSPHORYLATION AT THR-1224, INTERACTION WITH PRKCD, FUNCTION, AND
MUTAGENESIS OF SER-1223; THR-1224 AND SER-1227.
PubMed=11877440; DOI=10.1074/jbc.m200436200;
Ren J., Li Y., Kufe D.;
"Protein kinase C delta regulates function of the DF3/MUC1 carcinoma
antigen in beta-catenin signaling.";
J. Biol. Chem. 277:17616-17622(2002).
[44]
PHOSPHORYLATION AT TYR-1203; TYR-1212; TYR-1229 AND TYR-1243.
PubMed=14521915; DOI=10.1016/j.bbrc.2003.09.030;
Wang H., Lillehoj E.P., Kim K.C.;
"Identification of four sites of stimulated tyrosine phosphorylation in the
MUC1 cytoplasmic tail.";
Biochem. Biophys. Res. Commun. 310:341-346(2003).
[45]
INTERACTION WITH LYN, AND PHOSPHORYLATION.
PubMed=12750561; DOI=10.4161/cbt.2.2.282;
Li Y., Chen W., Ren J., Yu W.H., Li Q., Yoshida K., Kufe D.;
"DF3/MUC1 signaling in multiple myeloma cells is regulated by interleukin-
7.";
Cancer Biol. Ther. 2:187-193(2003).
[46]
INTERACTION WITH CTNNB1, FUNCTION, AND MUTAGENESIS OF TYR-1229.
PubMed=14688481;
Huang L., Ren J., Chen D., Li Y., Kharbanda S., Kufe D.;
"MUC1 cytoplasmic domain coactivates Wnt target gene transcription and
confers transformation.";
Cancer Biol. Ther. 2:702-706(2003).
[47]
INTERACTION WITH ADAM17, AND CLEAVAGE.
PubMed=12441351; DOI=10.1074/jbc.m208326200;
Thathiah A., Blobel C.P., Carson D.D.;
"Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1
shedding.";
J. Biol. Chem. 278:3386-3394(2003).
[48]
INTERACTION WITH CTNNB1, AND SUBCELLULAR LOCATION.
PubMed=12832415; DOI=10.1074/jbc.m304333200;
Wen Y., Caffrey T.C., Wheelock M.J., Johnson K.R., Hollingsworth M.A.;
"Nuclear association of the cytoplasmic tail of MUC1 and beta-catenin.";
J. Biol. Chem. 278:38029-38039(2003).
[49]
INTERACTION WITH ERBB2; ERBB3 AND ERBB4, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 1187-ARG--LYS-1189.
PubMed=12939402;
Li Y., Yu W.-H., Ren J., Chen W., Huang L., Kharbanda S., Loda M., Kufe D.;
"Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent
on the DF3/MUC1 oncoprotein.";
Mol. Cancer Res. 1:765-775(2003).
[50]
INTERACTION WITH AP1S2 AND GRB2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
TYR-1191; TYR-1203; TYR-1229 AND TYR-1243.
PubMed=15471854; DOI=10.1074/jbc.m409360200;
Kinlough C.L., Poland P.A., Bruns J.B., Harkleroad K.L., Hughey R.P.;
"MUC1 membrane trafficking is modulated by multiple interactions.";
J. Biol. Chem. 279:53071-53077(2004).
[51]
INTERACTION WITH TP53, AND FUNCTION.
PubMed=15710329; DOI=10.1016/j.ccr.2005.01.008;
Wei X., Xu H., Kufe D.;
"Human MUC1 oncoprotein regulates p53-responsive gene transcription in the
genotoxic stress response.";
Cancer Cell 7:167-178(2005).
[52]
INTERACTION WITH GSK3B, PHOSPHORYLATION, AND FUNCTION.
PubMed=16288032; DOI=10.1158/0008-5472.can-05-2474;
Huang L., Chen D., Liu D., Yin L., Kharbanda S., Kufe D.;
"MUC1 oncoprotein blocks glycogen synthase kinase 3beta-mediated
phosphorylation and degradation of beta-catenin.";
Cancer Res. 65:10413-10422(2005).
[53]
ERRATUM OF PUBMED:16288032.
Kinlough C.L., Poland P.A., Bruns J.B., Harkleroad K.L., Hughey R.P.;
J. Biol. Chem. 280:28827-28827(2005).
[54]
STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=15972891; DOI=10.1093/glycob/cwi099;
Engelmann K., Kinlough C.L., Muller S., Razawi H., Baldus S.E.,
Hughey R.P., Hanisch F.-G.;
"Transmembrane and secreted MUC1 probes show trafficking-dependent changes
in O-glycan core profiles.";
Glycobiology 15:1111-1124(2005).
[55]
INTERACTION WITH LCK, PHOSPHORYLATION, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15513966; DOI=10.1189/jlb.0604333;
Mukherjee P., Tinder T.L., Basu G.D., Gendler S.J.;
"MUC1 (CD227) interacts with lck tyrosine kinase in Jurkat lymphoma cells
and normal T cells.";
J. Leukoc. Biol. 77:90-99(2005).
[56]
PALMITOYLATION AT CYS-1184 AND CYS-1186, SUBCELLULAR LOCATION, INTERACTION
WITH AP1S1 AND AP1S2, AND MUTAGENESIS OF CYS-1184; CYS-1186; TYR-1203 AND
1187-ARG--LYS-1189.
PubMed=16507569; DOI=10.1074/jbc.m512996200;
Kinlough C.L., McMahan R.J., Poland P.A., Bruns J.B., Harkleroad K.L.,
Stremple R.J., Kashlan O.B., Weixel K.M., Weisz O.A., Hughey R.P.;
"Recycling of MUC1 is dependent on its palmitoylation.";
J. Biol. Chem. 281:12112-12122(2006).
[57]
INTERACTION WITH ESR1.
PubMed=16427018; DOI=10.1016/j.molcel.2005.11.030;
Wei X., Xu H., Kufe D.;
"MUC1 oncoprotein stabilizes and activates estrogen receptor alpha.";
Mol. Cell 21:295-305(2006).
[58]
INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=17524503; DOI=10.1016/j.bbamcr.2007.04.009;
Lillehoj E.P., Lu W., Kiser T., Goldblum S.E., Kim K.C.;
"MUC1 inhibits cell proliferation by a beta-catenin-dependent mechanism.";
Biochim. Biophys. Acta 1773:1028-1038(2007).
[59]
INTERACTION WITH KLF4, AND FUNCTION.
PubMed=17308127; DOI=10.1158/0008-5472.can-06-3063;
Wei X., Xu H., Kufe D.;
"Human mucin 1 oncoprotein represses transcription of the p53 tumor
suppressor gene.";
Cancer Res. 67:1853-1858(2007).
[60]
PHOSPHORYLATION AT TYR-1203; TYR-1218 AND TYR-1229, MUTAGENESIS OF TYR-1203
AND TYR-1218, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=17545600; DOI=10.1158/0008-5472.can-06-4647;
Singh P.K., Wen Y., Swanson B.J., Shanmugam K., Kazlauskas A., Cerny R.L.,
Gendler S.J., Hollingsworth M.A.;
"Platelet-derived growth factor receptor beta-mediated phosphorylation of
MUC1 enhances invasiveness in pancreatic adenocarcinoma cells.";
Cancer Res. 67:5201-5210(2007).
[61]
INTERACTION WITH EGFR, AND FUNCTION.
PubMed=16983337; DOI=10.1038/sj.onc.1209976;
Pochampalli M.R., el Bejjani R.M., Schroeder J.A.;
"MUC1 is a novel regulator of ErbB1 receptor trafficking.";
Oncogene 26:1693-1701(2007).
[62]
MARKER IN BREAST CANCER.
PubMed=20816948; DOI=10.1016/j.cca.2010.08.039;
Duffy M.J., Evoy D., McDermott E.W.;
"CA 15-3: uses and limitation as a biomarker for breast cancer.";
Clin. Chim. Acta 411:1869-1874(2010).
[63]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1227, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[64]
INVOLVEMENT IN MCKD1.
PubMed=23396133; DOI=10.1038/ng.2543;
Kirby A., Gnirke A., Jaffe D.B., Baresova V., Pochet N., Blumenstiel B.,
Ye C., Aird D., Stevens C., Robinson J.T., Cabili M.N., Gat-Viks I.,
Kelliher E., Daza R., DeFelice M., Hulkova H., Sovova J., Vylet'al P.,
Antignac C., Guttman M., Handsaker R.E., Perrin D., Steelman S.,
Sigurdsson S., Scheinman S.J., Sougnez C., Cibulskis K., Parkin M.,
Green T., Rossin E., Zody M.C., Xavier R.J., Pollak M.R., Alper S.L.,
Lindblad-Toh K., Gabriel S., Hart P.S., Regev A., Nusbaum C., Kmoch S.,
Bleyer A.J., Lander E.S., Daly M.J.;
"Mutations causing medullary cystic kidney disease type 1 lie in a large
VNTR in MUC1 missed by massively parallel sequencing.";
Nat. Genet. 45:299-303(2013).
[65]
STRUCTURE BY NMR OF 1041-1097 AND 1098-1152 OF WILD TYPE AND MUTANT
ALA-1098, IDENTIFICATION BY MASS SPECTROMETRY, STRUCTURE OF CARBOHYDRATES,
AND AUTOCATALYTIC CLEAVAGE.
PubMed=16585136; DOI=10.1093/glycob/cwj110;
Parry S., Hanisch F.G., Leir S.H., Sutton-Smith M., Morris H.R., Dell A.,
Harris A.;
"N-glycosylation of the MUC1 mucin in epithelial cells and secretions.";
Glycobiology 16:623-634(2006).
-!- FUNCTION: The alpha subunit has cell adhesive properties. Can act both
as an adhesion and an anti-adhesion protein. May provide a protective
layer on epithelial cells against bacterial and enzyme attack.
-!- FUNCTION: The beta subunit contains a C-terminal domain which is
involved in cell signaling, through phosphorylations and protein-
protein interactions. Modulates signaling in ERK, SRC and NF-kappa-B
pathways. In activated T-cells, influences directly or indirectly the
Ras/MAPK pathway. Promotes tumor progression. Regulates TP53-mediated
transcription and determines cell fate in the genotoxic stress
response. Binds, together with KLF4, the PE21 promoter element of TP53
and represses TP53 activity.
-!- SUBUNIT: The alpha subunit forms a tight, non-covalent heterodimeric
complex with the proteolytically-released beta-subunit. Interaction,
via the tandem repeat region, with domain 1 of ICAM1 is implicated in
cell migration and metastases. Isoform 1 binds directly the SH2 domain
of GRB2, and forms a MUC1/GRB2/SOS1 complex involved in RAS signaling.
The cytoplasmic tail (MUC1CT) interacts with several proteins such as
SRC, CTNNB1 and ERBs. Interaction with the SH2 domain of CSK decreases
interaction with GSK3B. Interacts with CTNNB1/beta-catenin and
JUP/gamma-catenin and promotes cell adhesion. Interaction with
JUP/gamma-catenin is induced by heregulin. Binds PRKCD, ERBB2, ERBB3
and ERBB4. Heregulin (HRG) stimulates the interaction with ERBB2 and,
to a much lesser extent, the interaction with ERBB3 and ERBB4.
Interacts with P53 in response to DNA damage. Interacts with KLF4.
Interacts with estrogen receptor alpha/ESR1, through its DNA-binding
domain, and stimulates its transcription activity. Binds ADAM17.
Isoform ZD forms disulfide-linked oligomers.
{ECO:0000269|PubMed:11152665, ECO:0000269|PubMed:11173916,
ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:11877440,
ECO:0000269|PubMed:12441351, ECO:0000269|PubMed:12750561,
ECO:0000269|PubMed:12832415, ECO:0000269|PubMed:12939402,
ECO:0000269|PubMed:14688481, ECO:0000269|PubMed:15471854,
ECO:0000269|PubMed:15513966, ECO:0000269|PubMed:15710329,
ECO:0000269|PubMed:16288032, ECO:0000269|PubMed:16427018,
ECO:0000269|PubMed:16507569, ECO:0000269|PubMed:16983337,
ECO:0000269|PubMed:17308127, ECO:0000269|PubMed:17524503,
ECO:0000269|PubMed:7664271, ECO:0000269|PubMed:9139698,
ECO:0000269|PubMed:9819408}.
-!- INTERACTION:
P15941; P00519: ABL1; NbExp=8; IntAct=EBI-2804728, EBI-375543;
P15941; P00533: EGFR; NbExp=4; IntAct=EBI-2804728, EBI-297353;
P15941; P08581: MET; NbExp=2; IntAct=EBI-2804728, EBI-1039152;
P15941; P15941-7: MUC1; NbExp=2; IntAct=EBI-2804728, EBI-4396776;
P15941-11; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-17263240, EBI-10225815;
P15941-11; O60242: ADGRB3; NbExp=3; IntAct=EBI-17263240, EBI-2682765;
P15941-11; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-17263240, EBI-10827839;
P15941-11; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-17263240, EBI-12109402;
P15941-11; P02652: APOA2; NbExp=3; IntAct=EBI-17263240, EBI-1171525;
P15941-11; P05067-2: APP; NbExp=3; IntAct=EBI-17263240, EBI-17264467;
P15941-11; P29972: AQP1; NbExp=3; IntAct=EBI-17263240, EBI-745213;
P15941-11; P41181: AQP2; NbExp=3; IntAct=EBI-17263240, EBI-12701138;
P15941-11; Q92482: AQP3; NbExp=3; IntAct=EBI-17263240, EBI-2808854;
P15941-11; Q9H2C2: ARV1; NbExp=3; IntAct=EBI-17263240, EBI-11724186;
P15941-11; Q92843: BCL2L2; NbExp=3; IntAct=EBI-17263240, EBI-707714;
P15941-11; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-17263240, EBI-12244618;
P15941-11; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-17263240, EBI-8648738;
P15941-11; P06681: C2; NbExp=3; IntAct=EBI-17263240, EBI-2835920;
P15941-11; O14523: C2CD2L; NbExp=3; IntAct=EBI-17263240, EBI-12822627;
P15941-11; Q06432: CACNG1; NbExp=3; IntAct=EBI-17263240, EBI-9686780;
P15941-11; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-17263240, EBI-9083477;
P15941-11; Q08722-3: CD47; NbExp=3; IntAct=EBI-17263240, EBI-17263290;
P15941-11; P19397: CD53; NbExp=3; IntAct=EBI-17263240, EBI-6657396;
P15941-11; P34810: CD68; NbExp=3; IntAct=EBI-17263240, EBI-2826276;
P15941-11; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-17263240, EBI-12256978;
P15941-11; P56747: CLDN6; NbExp=3; IntAct=EBI-17263240, EBI-12955011;
P15941-11; Q8NHS1: CLDND2; NbExp=3; IntAct=EBI-17263240, EBI-11959453;
P15941-11; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-17263240, EBI-2807956;
P15941-11; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-17263240, EBI-10241815;
P15941-11; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-17263240, EBI-10267100;
P15941-11; A0A6I8PIU0: CXCL16; NbExp=3; IntAct=EBI-17263240, EBI-10176529;
P15941-11; Q07325: CXCL9; NbExp=3; IntAct=EBI-17263240, EBI-3911467;
P15941-11; O43169: CYB5B; NbExp=3; IntAct=EBI-17263240, EBI-1058710;
P15941-11; P78329: CYP4F2; NbExp=3; IntAct=EBI-17263240, EBI-1752413;
P15941-11; P56851: EDDM3B; NbExp=3; IntAct=EBI-17263240, EBI-10215665;
P15941-11; Q9BV81: EMC6; NbExp=3; IntAct=EBI-17263240, EBI-2820492;
P15941-11; P54852: EMP3; NbExp=3; IntAct=EBI-17263240, EBI-3907816;
P15941-11; O75355-2: ENTPD3; NbExp=3; IntAct=EBI-17263240, EBI-12279764;
P15941-11; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-17263240, EBI-711490;
P15941-11; P01350: GAST; NbExp=3; IntAct=EBI-17263240, EBI-3436637;
P15941-11; P39905-3: GDNF; NbExp=3; IntAct=EBI-17263240, EBI-12702062;
P15941-11; Q9Y3E0: GOLT1B; NbExp=3; IntAct=EBI-17263240, EBI-4402607;
P15941-11; Q9NPR9: GPR108; NbExp=3; IntAct=EBI-17263240, EBI-11343451;
P15941-11; Q9HCP6: HHATL; NbExp=3; IntAct=EBI-17263240, EBI-5916693;
P15941-11; O60725: ICMT; NbExp=3; IntAct=EBI-17263240, EBI-11721771;
P15941-11; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-17263240, EBI-8503746;
P15941-11; P11215: ITGAM; NbExp=3; IntAct=EBI-17263240, EBI-2568251;
P15941-11; Q969L2: MAL2; NbExp=3; IntAct=EBI-17263240, EBI-944295;
P15941-11; Q13021: MALL; NbExp=3; IntAct=EBI-17263240, EBI-750078;
P15941-11; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-17263240, EBI-10317612;
P15941-11; Q6N075: MFSD5; NbExp=3; IntAct=EBI-17263240, EBI-3920969;
P15941-11; P30301: MIP; NbExp=3; IntAct=EBI-17263240, EBI-8449636;
P15941-11; Q96S97: MYADM; NbExp=3; IntAct=EBI-17263240, EBI-13301517;
P15941-11; O95167: NDUFA3; NbExp=3; IntAct=EBI-17263240, EBI-1246131;
P15941-11; Q99519: NEU1; NbExp=3; IntAct=EBI-17263240, EBI-721517;
P15941-11; Q92982: NINJ1; NbExp=3; IntAct=EBI-17263240, EBI-2802124;
P15941-11; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-17263240, EBI-10317425;
P15941-11; Q16617: NKG7; NbExp=3; IntAct=EBI-17263240, EBI-3919611;
P15941-11; Q8N912: NRAC; NbExp=3; IntAct=EBI-17263240, EBI-12051377;
P15941-11; Q8NH19: OR10AG1; NbExp=3; IntAct=EBI-17263240, EBI-13339917;
P15941-11; Q6TCH4: PAQR6; NbExp=3; IntAct=EBI-17263240, EBI-17265310;
P15941-11; P26678: PLN; NbExp=3; IntAct=EBI-17263240, EBI-692836;
P15941-11; P60201-2: PLP1; NbExp=3; IntAct=EBI-17263240, EBI-12188331;
P15941-11; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-17263240, EBI-11721828;
P15941-11; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-17263240, EBI-8652812;
P15941-11; Q59EV6: PPGB; NbExp=3; IntAct=EBI-17263240, EBI-14210385;
P15941-11; P30405: PPIF; NbExp=3; IntAct=EBI-17263240, EBI-5544229;
P15941-11; Q96AA3: RFT1; NbExp=3; IntAct=EBI-17263240, EBI-6269616;
P15941-11; Q02161-2: RHD; NbExp=3; IntAct=EBI-17263240, EBI-17249212;
P15941-11; Q8TAC9: SCAMP5; NbExp=3; IntAct=EBI-17263240, EBI-2695784;
P15941-11; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-17263240, EBI-9679163;
P15941-11; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-17263240, EBI-749270;
P15941-11; P11686: SFTPC; NbExp=3; IntAct=EBI-17263240, EBI-10197617;
P15941-11; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-17263240, EBI-10262251;
P15941-11; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-17263240, EBI-10281213;
P15941-11; Q6ICL7: SLC35E4; NbExp=3; IntAct=EBI-17263240, EBI-12867720;
P15941-11; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-17263240, EBI-10314552;
P15941-11; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-17263240, EBI-8640191;
P15941-11; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-17263240, EBI-12188413;
P15941-11; Q9NZ01: TECR; NbExp=3; IntAct=EBI-17263240, EBI-2877718;
P15941-11; P07204: THBD; NbExp=3; IntAct=EBI-17263240, EBI-941422;
P15941-11; Q9BZW4: TM6SF2; NbExp=3; IntAct=EBI-17263240, EBI-13082040;
P15941-11; P17152: TMEM11; NbExp=3; IntAct=EBI-17263240, EBI-723946;
P15941-11; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-17263240, EBI-10171534;
P15941-11; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-17263240, EBI-12155101;
P15941-11; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-17263240, EBI-10694905;
P15941-11; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-17263240, EBI-348587;
P15941-11; Q9Y6G1: TMEM14A; NbExp=3; IntAct=EBI-17263240, EBI-2800360;
P15941-11; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-17263240, EBI-2339195;
P15941-11; Q14656: TMEM187; NbExp=3; IntAct=EBI-17263240, EBI-13046724;
P15941-11; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-17263240, EBI-12195227;
P15941-11; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-17263240, EBI-12887458;
P15941-11; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-17263240, EBI-12015604;
P15941-11; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-17263240, EBI-2548832;
P15941-11; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-17263240, EBI-12111910;
P15941-11; Q9Y2Y6: TMEM98; NbExp=3; IntAct=EBI-17263240, EBI-7333781;
P15941-11; O14763: TNFRSF10B; NbExp=3; IntAct=EBI-17263240, EBI-518882;
P15941-11; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-17263240, EBI-11996766;
P15941-11; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-17263240, EBI-10243654;
P15941-11; Q53HI1: UNC50; NbExp=3; IntAct=EBI-17263240, EBI-7601760;
P15941-11; O95183: VAMP5; NbExp=3; IntAct=EBI-17263240, EBI-10191195;
P15941-11; Q9BQB6: VKORC1; NbExp=3; IntAct=EBI-17263240, EBI-6256462;
P15941-11; Q8IVQ6: ZDHHC21; NbExp=3; IntAct=EBI-17263240, EBI-2849773;
PRO_0000317447; P17676: CEBPB; NbExp=8; IntAct=EBI-10053698, EBI-969696;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:11118479, ECO:0000269|PubMed:12832415,
ECO:0000269|PubMed:12939402, ECO:0000269|PubMed:15471854,
ECO:0000269|PubMed:15972891, ECO:0000269|PubMed:16507569,
ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:17545600}; Single-pass
type I membrane protein {ECO:0000269|PubMed:11118479,
ECO:0000269|PubMed:12832415, ECO:0000269|PubMed:12939402,
ECO:0000269|PubMed:15471854, ECO:0000269|PubMed:15972891,
ECO:0000269|PubMed:16507569, ECO:0000269|PubMed:17524503,
ECO:0000269|PubMed:17545600}. Note=Exclusively located in the apical
domain of the plasma membrane of highly polarized epithelial cells.
After endocytosis, internalized and recycled to the cell membrane.
Located to microvilli and to the tips of long filopodial protusions.
-!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted.
-!- SUBCELLULAR LOCATION: [Isoform Y]: Secreted.
-!- SUBCELLULAR LOCATION: [Isoform 9]: Secreted.
-!- SUBCELLULAR LOCATION: [Mucin-1 subunit beta]: Cell membrane. Cytoplasm.
Nucleus. Note=On EGF and PDGFRB stimulation, transported to the nucleus
through interaction with CTNNB1, a process which is stimulated by
phosphorylation. On HRG stimulation, colocalizes with JUP/gamma-catenin
at the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=17;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=A;
IsoId=P15941-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=P15941-2; Sequence=VSP_003280;
Name=3; Synonyms=C;
IsoId=P15941-3; Sequence=VSP_003281;
Name=4; Synonyms=D;
IsoId=P15941-4; Sequence=VSP_003282;
Name=5; Synonyms=SEC;
IsoId=P15941-5; Sequence=VSP_003288, VSP_003289;
Name=6; Synonyms=X;
IsoId=P15941-6; Sequence=VSP_003283, VSP_003284;
Name=Y; Synonyms=MUC1/Y;
IsoId=P15941-7; Sequence=VSP_003285;
Name=8; Synonyms=Z;
IsoId=P15941-8; Sequence=VSP_003286;
Name=9; Synonyms=S;
IsoId=P15941-9; Sequence=VSP_003286, VSP_003287;
Name=F;
IsoId=P15941-10; Sequence=VSP_035046, VSP_035047;
Name=Y-LSP;
IsoId=P15941-11; Sequence=VSP_003280, VSP_003285;
Name=S2;
IsoId=P15941-12; Sequence=VSP_003280, VSP_003285, VSP_003287;
Name=M6;
IsoId=P15941-13; Sequence=VSP_003286, VSP_046962, VSP_046963;
Name=ZD; Synonyms=J19;
IsoId=P15941-14; Sequence=VSP_047575, VSP_047576;
Name=T10;
IsoId=P15941-15; Sequence=VSP_003280, VSP_047873;
Name=E2;
IsoId=P15941-16; Sequence=VSP_003280, VSP_047872;
Name=J13;
IsoId=P15941-17; Sequence=VSP_003280, VSP_003285, VSP_047874;
-!- TISSUE SPECIFICITY: Expressed on the apical surface of epithelial
cells, especially of airway passages, breast and uterus. Also expressed
in activated and unactivated T-cells. Overexpressed in epithelial
tumors, such as breast or ovarian cancer and also in non-epithelial
tumor cells. Isoform Y is expressed in tumor cells only.
{ECO:0000269|PubMed:15513966, ECO:0000269|PubMed:9212228}.
-!- DEVELOPMENTAL STAGE: During fetal development, expressed at low levels
in the colonic epithelium from 13 weeks of gestation.
{ECO:0000269|PubMed:9536947}.
-!- PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic
acid). O-glycosylated to a varying degree on serine and threonine
residues within each tandem repeat, ranging from mono- to penta-
glycosylation. The average density ranges from about 50% in human milk
to over 90% in T47D breast cancer cells. Further sialylation occurs
during recycling. Membrane-shed glycoproteins from kidney and breast
cancer cells have preferentially sialyated core 1 structures, while
secreted forms from the same tissues display mainly core 2 structures.
The O-glycosylated content is overlapping in both these tissues with
terminal fucose and galactose, 2- and 3-linked galactose, 3- and 3,6-
linked GalNAc-ol and 4-linked GlcNAc predominating. Differentially O-
glycosylated in breast carcinomas with 3,4-linked GlcNAc. N-
glycosylation consists of high-mannose, acidic complex-type and hybrid
glycans in the secreted form MUC1/SEC, and neutral complex-type in the
transmembrane form, MUC1/TM. {ECO:0000269|PubMed:10373415,
ECO:0000269|PubMed:7744025, ECO:0000269|PubMed:9312074,
ECO:0000269|PubMed:9597769}.
-!- PTM: Proteolytic cleavage in the SEA domain occurs in the endoplasmic
reticulum by an autoproteolytic mechanism and requires the full-length
SEA domain as well as requiring a Ser, Thr or Cys residue at the P + 1
site. Cleavage at this site also occurs on isoform MUC1/X but not on
isoform MUC1/Y. Ectodomain shedding is mediated by ADAM17.
{ECO:0000269|PubMed:11341784, ECO:0000269|PubMed:12441351,
ECO:0000269|PubMed:15987679}.
-!- PTM: Dual palmitoylation on cysteine residues in the CQC motif is
required for recycling from endosomes back to the plasma membrane.
{ECO:0000269|PubMed:16507569}.
-!- PTM: Phosphorylated on tyrosines and serine residues in the C-terminal.
Phosphorylation on tyrosines in the C-terminal increases the nuclear
location of MUC1 and beta-catenin. Phosphorylation by PKC delta induces
binding of MUC1 to beta-catenin/CTNNB1 and thus decreases the formation
of the beta-catenin/E-cadherin complex. Src-mediated phosphorylation
inhibits interaction with GSK3B. Src- and EGFR-mediated phosphorylation
on Tyr-1229 increases binding to beta-catenin/CTNNB1. GSK3B-mediated
phosphorylation on Ser-1227 decreases this interaction but restores the
formation of the beta-cadherin/E-cadherin complex. On T-cell receptor
activation, phosphorylated by LCK. PDGFR-mediated phosphorylation
increases nuclear colocalization of MUC1CT and CTNNB1.
{ECO:0000269|PubMed:11152665, ECO:0000269|PubMed:11483589,
ECO:0000269|PubMed:11877440, ECO:0000269|PubMed:12750561,
ECO:0000269|PubMed:14521915, ECO:0000269|PubMed:15513966,
ECO:0000269|PubMed:16288032, ECO:0000269|PubMed:17545600,
ECO:0000269|PubMed:7664271, ECO:0000269|PubMed:7988707,
ECO:0000269|PubMed:9819408}.
-!- PTM: The N-terminal sequence has been shown to begin at position 24 or
28. {ECO:0000269|PubMed:11341784}.
-!- POLYMORPHISM: The number of repeats is highly polymorphic. It varies
from 21 to 125 in the northern European population. The most frequent
alleles contains 41 and 85 repeats. The tandemly repeated icosapeptide
underlies polymorphism at three positions:
PAPGSTAP[PAQT]AHGVTSAP[DT/ES]R, DT -> ES and the single replacements P
-> A, P -> Q and P-> T. The most frequent replacement DT -> ES occurs
in up to 50% of the repeats.
-!- DISEASE: Note=MUC1/CA 15-3 is used as a serological clinical marker of
breast cancer to monitor response to breast cancer treatment and
disease recurrence (PubMed:20816948). Decreased levels over time may be
indicative of a positive response to treatment. Conversely, increased
levels may indicate disease progression. At an early stage disease,
only 21% of patients exhibit high MUC1/CA 15-3 levels, that is why CA
15-3 is not a useful screening test. Most antibodies target the highly
immunodominant core peptide domain of 20 amino acid
(APDTRPAPGSTAPPAHGVTS) tandem repeats. Some antibodies recognize
glycosylated epitopes. {ECO:0000269|PubMed:20816948}.
-!- DISEASE: Medullary cystic kidney disease 1 (MCKD1) [MIM:174000]: A form
of tubulointerstitial nephropathy characterized by formation of renal
cysts at the corticomedullary junction. It is characterized by adult
onset of impaired renal function and salt wasting resulting in end-
stage renal failure by the sixth decade. {ECO:0000269|PubMed:23396133}.
Note=The disease is caused by variants affecting the gene represented
in this entry.
-!- MISCELLANEOUS: The name KL-6 was originally that of a murine monoclonal
antibody reacting with pulmonary adenocarcinoma cell lines and
pulmonary epithelial cells. This antibody recognizes a sialylated
carbohydrate chain on MUC1.
-!- MISCELLANEOUS: [Isoform Y-LSP]: Lacks the mucin repeats. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform ZD]: Lacks the mucin repeats. Exists as a
disulfide-linked oligomer. {ECO:0000305}.
-!- CAUTION: O-glycosylation sites are annotated in first sequence repeat
only. Residues at similar position are probably glycosylated in all
repeats. Experimental sites were determined in a synthetic peptide
glycosylated in vitro (PubMed:7744025, PubMed:9597769).
{ECO:0000305|PubMed:7744025, ECO:0000305|PubMed:9597769}.
-!- SEQUENCE CAUTION:
Sequence=AAD14369.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
Sequence=AAD14376.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Mucin database;
URL="http://www.medkem.gu.se/mucinbiology/databases/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/muc1/";
---------------------------------------------------------------------------
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EMBL; J05582; AAA60019.1; -; mRNA.
EMBL; M32738; AAA35804.1; -; mRNA.
EMBL; M32739; AAA35806.1; -; mRNA.
EMBL; M34089; AAA35807.1; -; mRNA.
EMBL; M34088; AAA35805.1; -; mRNA.
EMBL; J05581; AAA59876.1; -; mRNA.
EMBL; M61170; AAB53150.1; -; Genomic_DNA.
EMBL; X52229; CAA36478.1; ALT_SEQ; mRNA.
EMBL; X52228; CAA36477.1; ALT_SEQ; mRNA.
EMBL; M35093; AAB59612.1; ALT_SEQ; Genomic_DNA.
EMBL; X80761; CAA56734.1; -; mRNA.
EMBL; U60259; AAD10856.1; -; mRNA.
EMBL; U60260; AAD10857.1; -; mRNA.
EMBL; U60261; AAD10858.1; -; mRNA.
EMBL; AF125525; AAD27842.1; -; mRNA.
EMBL; AY466157; AAR28764.1; -; mRNA.
EMBL; AY327582; AAP97013.1; -; mRNA.
EMBL; AY327584; AAP97015.1; -; mRNA.
EMBL; AY327586; AAP97017.1; -; mRNA.
EMBL; AY327587; AAP97018.1; -; mRNA.
EMBL; EF583653; ABQ59628.1; -; mRNA.
EMBL; EF670711; ABS01298.1; -; mRNA.
EMBL; EF670712; ABS01299.1; -; mRNA.
EMBL; FJ226040; ACI25172.1; -; mRNA.
EMBL; FJ226047; ACI25179.1; -; mRNA.
EMBL; AF348143; AAK30142.1; -; mRNA.
EMBL; AY463543; AAR18816.1; -; Genomic_DNA.
EMBL; AL713999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53116.1; -; Genomic_DNA.
EMBL; CH471121; EAW53117.1; -; Genomic_DNA.
EMBL; CH471121; EAW53118.1; -; Genomic_DNA.
EMBL; CH471121; EAW53119.1; -; Genomic_DNA.
EMBL; BC120974; AAI20975.1; -; mRNA.
EMBL; BC120975; AAI20976.1; -; mRNA.
EMBL; Z17324; CAA78972.1; -; mRNA.
EMBL; Z17325; CAA78973.1; -; mRNA.
EMBL; M31823; AAA35757.1; -; mRNA.
EMBL; S81781; AAD14376.1; ALT_INIT; mRNA.
EMBL; S81736; AAD14369.1; ALT_INIT; mRNA.
EMBL; M21868; AAA59874.1; ALT_SEQ; mRNA.
CCDS; CCDS1098.1; -. [P15941-8]
CCDS; CCDS30882.1; -. [P15941-11]
CCDS; CCDS30883.1; -. [P15941-7]
CCDS; CCDS41408.1; -. [P15941-12]
CCDS; CCDS41409.1; -. [P15941-10]
CCDS; CCDS55641.1; -. [P15941-6]
CCDS; CCDS55642.1; -. [P15941-13]
PIR; A35175; A35175.
RefSeq; NP_001018016.1; NM_001018016.2. [P15941-11]
RefSeq; NP_001018017.1; NM_001018017.2. [P15941-7]
RefSeq; NP_001037855.1; NM_001044390.2. [P15941-10]
RefSeq; NP_001037856.1; NM_001044391.2.
RefSeq; NP_001037857.1; NM_001044392.2. [P15941-12]
RefSeq; NP_001037858.1; NM_001044393.2.
RefSeq; NP_001191214.1; NM_001204285.1.
RefSeq; NP_001191215.1; NM_001204286.1.
RefSeq; NP_001191216.1; NM_001204287.1.
RefSeq; NP_001191217.1; NM_001204288.1.
RefSeq; NP_001191218.1; NM_001204289.1.
RefSeq; NP_001191219.1; NM_001204290.1.
RefSeq; NP_001191220.1; NM_001204291.1.
RefSeq; NP_001191221.1; NM_001204292.1.
RefSeq; NP_001191222.1; NM_001204293.1. [P15941-13]
RefSeq; NP_001191223.1; NM_001204294.1. [P15941-6]
RefSeq; NP_001191224.1; NM_001204295.1.
RefSeq; NP_001191225.1; NM_001204296.1.
RefSeq; NP_001191226.1; NM_001204297.1.
RefSeq; NP_002447.4; NM_002456.5. [P15941-8]
PDB; 1SM3; X-ray; 1.95 A; P=919-931.
PDB; 2ACM; NMR; -; A=1042-1097, B=1098-1152.
PDB; 2FO4; X-ray; 2.70 A; P=140-146.
PDB; 5T6P; X-ray; 1.97 A; E/F=921-928.
PDB; 5T78; X-ray; 2.20 A; E/F=921-928.
PDB; 6FZQ; X-ray; 1.70 A; P=921-926.
PDB; 6FZR; X-ray; 1.80 A; P=921-926.
PDB; 6KX1; X-ray; 1.77 A; C=918-932.
PDB; 6TGG; X-ray; 2.00 A; P=921-926.
PDBsum; 1SM3; -.
PDBsum; 2ACM; -.
PDBsum; 2FO4; -.
PDBsum; 5T6P; -.
PDBsum; 5T78; -.
PDBsum; 6FZQ; -.
PDBsum; 6FZR; -.
PDBsum; 6KX1; -.
PDBsum; 6TGG; -.
SMR; P15941; -.
BioGRID; 110669; 148.
DIP; DIP-41890N; -.
IntAct; P15941; 122.
MINT; P15941; -.
STRING; 9606.ENSP00000484824; -.
ChEMBL; CHEMBL3580494; -.
DrugBank; DB11090; Potassium nitrate.
DrugBank; DB06584; TG4010.
MEROPS; S71.001; -.
GlyConnect; 372; 9 O-Linked glycans.
GlyConnect; 373; 8 O-Linked glycans.
GlyConnect; 374; 7 N-Linked glycans (3 sites), 8 O-Linked glycans.
GlyConnect; 375; 10 O-Linked glycans.
GlyConnect; 376; 10 O-Linked glycans.
GlyConnect; 377; 7 O-Linked glycans.
GlyConnect; 413; 5 N-Linked glycans (1 site), 14 O-Linked glycans.
GlyGen; P15941; 13 sites, 5 O-linked glycans (4 sites).
iPTMnet; P15941; -.
PhosphoSitePlus; P15941; -.
SwissPalm; P15941; -.
BioMuta; MUC1; -.
DMDM; 296439295; -.
CPTAC; CPTAC-146; -.
CPTAC; CPTAC-147; -.
CPTAC; CPTAC-719; -.
CPTAC; CPTAC-730; -.
jPOST; P15941; -.
MassIVE; P15941; -.
MaxQB; P15941; -.
PaxDb; P15941; -.
PeptideAtlas; P15941; -.
PRIDE; P15941; -.
ProteomicsDB; 1779; -.
ProteomicsDB; 53249; -. [P15941-1]
ProteomicsDB; 53250; -. [P15941-10]
ProteomicsDB; 53251; -. [P15941-2]
ProteomicsDB; 53252; -. [P15941-3]
ProteomicsDB; 53253; -. [P15941-4]
ProteomicsDB; 53254; -. [P15941-5]
ProteomicsDB; 53255; -. [P15941-6]
ProteomicsDB; 53256; -. [P15941-7]
ProteomicsDB; 53257; -. [P15941-8]
ProteomicsDB; 53258; -. [P15941-9]
ProteomicsDB; 58806; -.
ProteomicsDB; 6245; -.
ProteomicsDB; 69255; -.
ProteomicsDB; 69256; -.
ProteomicsDB; 767; -.
ABCD; P15941; 33 sequenced antibodies.
Antibodypedia; 1298; 4494 antibodies.
CPTC; P15941; 2 antibodies.
DNASU; 4582; -.
Ensembl; ENST00000337604; ENSP00000338983; ENSG00000185499. [P15941-8]
Ensembl; ENST00000342482; ENSP00000342814; ENSG00000185499. [P15941-16]
Ensembl; ENST00000343256; ENSP00000339690; ENSG00000185499. [P15941-10]
Ensembl; ENST00000368389; ENSP00000357374; ENSG00000185499. [P15941-9]
Ensembl; ENST00000368390; ENSP00000357375; ENSG00000185499. [P15941-7]
Ensembl; ENST00000368392; ENSP00000357377; ENSG00000185499. [P15941-11]
Ensembl; ENST00000368393; ENSP00000357378; ENSG00000185499. [P15941-13]
Ensembl; ENST00000368396; ENSP00000357381; ENSG00000185499. [P15941-12]
Ensembl; ENST00000368398; ENSP00000357383; ENSG00000185499. [P15941-6]
GeneID; 4582; -.
KEGG; hsa:4582; -.
UCSC; uc001fia.4; human. [P15941-1]
CTD; 4582; -.
DisGeNET; 4582; -.
GeneCards; MUC1; -.
GeneReviews; MUC1; -.
HGNC; HGNC:7508; MUC1.
HPA; ENSG00000185499; Tissue enhanced (gallbladder, kidney, lung).
MalaCards; MUC1; -.
MIM; 113720; gene.
MIM; 158340; gene.
MIM; 174000; phenotype.
neXtProt; NX_P15941; -.
OpenTargets; ENSG00000185499; -.
Orphanet; 88949; MUC1-related autosomal dominant tubulointerstitial kidney disease.
PharmGKB; PA31309; -.
VEuPathDB; HostDB:ENSG00000185499.16; -.
eggNOG; ENOG502QWCT; Eukaryota.
GeneTree; ENSGT00940000167855; -.
HOGENOM; CLU_1386987_0_0_1; -.
InParanoid; P15941; -.
OrthoDB; 945460at2759; -.
PhylomeDB; P15941; -.
PathwayCommons; P15941; -.
Reactome; R-HSA-5083625; Defective GALNT3 causes familial hyperphosphatemic tumoral calcinosis (HFTC).
Reactome; R-HSA-5083632; Defective C1GALT1C1 causes Tn polyagglutination syndrome (TNPS).
Reactome; R-HSA-5083636; Defective GALNT12 causes colorectal cancer 1 (CRCS1).
Reactome; R-HSA-5621480; Dectin-2 family.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
SIGNOR; P15941; -.
BioGRID-ORCS; 4582; 6 hits in 997 CRISPR screens.
ChiTaRS; MUC1; human.
EvolutionaryTrace; P15941; -.
GeneWiki; MUC1; -.
GenomeRNAi; 4582; -.
Pharos; P15941; Tbio.
PRO; PR:P15941; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P15941; protein.
Bgee; ENSG00000185499; Expressed in body of stomach and 212 other tissues.
ExpressionAtlas; P15941; baseline and differential.
Genevisible; P15941; HS.
GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0003712; F:transcription coregulator activity; IDA:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IDA:BHF-UCL.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:BHF-UCL.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IDA:CACAO.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:BHF-UCL.
GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:BHF-UCL.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0090240; P:positive regulation of histone H4 acetylation; IDA:BHF-UCL.
GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IDA:BHF-UCL.
GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IDA:BHF-UCL.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DisProt; DP01790; -.
Gene3D; 3.30.70.960; -; 1.
IDEAL; IID00195; -.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
Pfam; PF01390; SEA; 1.
SMART; SM00200; SEA; 1.
SUPFAM; SSF82671; SSF82671; 1.
PROSITE; PS50024; SEA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Autocatalytic cleavage; Cell membrane;
Cytoplasm; Direct protein sequencing; Disulfide bond; Glycoprotein;
Lipoprotein; Membrane; Nucleus; Palmitate; Phosphoprotein;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix; Tumor suppressor.
SIGNAL 1..23
/evidence="ECO:0000269|PubMed:10373415,
ECO:0000269|PubMed:11341784"
CHAIN 24..1255
/note="Mucin-1"
/id="PRO_0000019277"
CHAIN 24..1097
/note="Mucin-1 subunit alpha"
/id="PRO_0000317446"
CHAIN 1098..1255
/note="Mucin-1 subunit beta"
/id="PRO_0000317447"
TOPO_DOM 24..1158
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 1159..1181
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1182..1255
/note="Cytoplasmic"
/evidence="ECO:0000255"
REPEAT 61..80
/note="1; approximate"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 81..100
/note="2; approximate"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 101..120
/note="3"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 121..140
/note="4"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 141..160
/note="5"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 161..180
/note="6"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 181..200
/note="7"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 201..220
/note="8"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 221..240
/note="9"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 241..260
/note="10"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 261..280
/note="11"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 281..300
/note="12"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 301..320
/note="13"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 321..340
/note="14"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 341..360
/note="15"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 361..380
/note="16"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 381..400
/note="17"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 401..420
/note="18"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 421..440
/note="19"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 441..460
/note="20"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 461..480
/note="21"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 481..500
/note="22"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 501..520
/note="23"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 521..540
/note="24"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 541..560
/note="25"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 561..580
/note="26"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 581..600
/note="27"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 601..620
/note="28"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 621..640
/note="29"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 641..660
/note="30"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 661..680
/note="31"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 681..700
/note="32"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 701..720
/note="33"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 721..740
/note="34"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 741..760
/note="35"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 761..780
/note="36"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 781..800
/note="37"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 801..820
/note="38"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 821..840
/note="39"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 841..860
/note="40"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 861..880
/note="41"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 881..900
/note="42"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 901..920
/note="43"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 921..940
/note="44"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 941..960
/note="45"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 961..980
/note="46; approximate"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 981..1000
/note="47; approximate"
/evidence="ECO:0000269|PubMed:11350974"
REPEAT 1001..1020
/note="48; approximate"
/evidence="ECO:0000269|PubMed:11350974"
DOMAIN 1039..1148
/note="SEA"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
REGION 126..965
/note="42 X 20 AA approximate tandem repeats of P-A-P-G-S-
T-A-P-P-A-H-G-V-T-S-A-P-D-T-R"
REGION 1192..1228
/note="Interaction with P53"
REGION 1223..1230
/note="Required for interaction with GSK3B"
REGION 1233..1241
/note="Required for interaction with beta- and gamma-
catenins"
MOTIF 1203..1206
/note="Interaction with GRB2"
MOTIF 1229..1232
/note="Interaction with SRC and ESR1"
MOTIF 1243..1246
/note="Required for interaction with AP1S2"
SITE 1097..1098
/note="Cleavage; by autolysis"
MOD_RES 1203
/note="Phosphotyrosine; by PDGFR"
/evidence="ECO:0000269|PubMed:14521915,
ECO:0000269|PubMed:17545600"
MOD_RES 1212
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:14521915"
MOD_RES 1218
/note="Phosphotyrosine; by PDGFR"
/evidence="ECO:0000269|PubMed:17545600"
MOD_RES 1224
/note="Phosphothreonine; by PKC/PRKCD"
/evidence="ECO:0000269|PubMed:11877440"
MOD_RES 1227
/note="Phosphoserine; by GSK3-beta"
/evidence="ECO:0000269|PubMed:9819408,
ECO:0007744|PubMed:23186163"
MOD_RES 1229
/note="Phosphotyrosine; by CSK, EGFR and SRC"
/evidence="ECO:0000269|PubMed:11152665,
ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:14521915,
ECO:0000269|PubMed:17545600"
MOD_RES 1243
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:14521915"
LIPID 1184
/note="S-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:16507569"
LIPID 1186
/note="S-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:16507569"
CARBOHYD 131
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000305|PubMed:7744025,
ECO:0000305|PubMed:9597769"
CARBOHYD 139
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000305|PubMed:7744025,
ECO:0000305|PubMed:9597769"
CARBOHYD 140
/note="O-linked (GalNAc...) serine"
/evidence="ECO:0000255"
CARBOHYD 144
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000255"
CARBOHYD 957
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 975
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1029
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1055
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1133
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
VAR_SEQ 19..21
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|Ref.25"
/id="VSP_003281"
VAR_SEQ 19
/note="T -> TATTAPKPAT (in isoform 2, isoform Y-LSP,
isoform E2, isoform J13, isoform S2 and isoform T10)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:22941036, ECO:0000303|PubMed:2318825,
ECO:0000303|PubMed:2597151, ECO:0000303|PubMed:8608966,
ECO:0000303|Ref.15"
/id="VSP_003280"
VAR_SEQ 20..31
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|Ref.25"
/id="VSP_003282"
VAR_SEQ 54..1151
/note="Missing (in isoform E2)"
/evidence="ECO:0000303|PubMed:22941036"
/id="VSP_047872"
VAR_SEQ 54..1093
/note="Missing (in isoform T10)"
/evidence="ECO:0000303|PubMed:22941036"
/id="VSP_047873"
VAR_SEQ 54..1053
/note="Missing (in isoform J13, isoform Y, isoform Y-LSP
and isoform S2)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15969018, ECO:0000303|PubMed:22941036,
ECO:0000303|PubMed:7925397, ECO:0000303|PubMed:9212228,
ECO:0000303|Ref.15"
/id="VSP_003285"
VAR_SEQ 54..1035
/note="Missing (in isoform 8, isoform 9 and isoform M6)"
/evidence="ECO:0000303|PubMed:22941036,
ECO:0000303|PubMed:9212228, ECO:0000303|Ref.12,
ECO:0000303|Ref.16"
/id="VSP_003286"
VAR_SEQ 54..96
/note="VSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQ -> IPAPT
TTKSCRETFLKCFCRFINKGVFWASPILSSGQDLWWYN (in isoform ZD)"
/evidence="ECO:0000303|PubMed:15623537,
ECO:0000303|PubMed:22941036"
/id="VSP_047575"
VAR_SEQ 54..87
/note="VSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPA -> IPAPTTTKSCRETF
LKCFCRFINKGVFWASPILS (in isoform F)"
/evidence="ECO:0000303|Ref.14"
/id="VSP_035046"
VAR_SEQ 54..70
/note="VSMTSSVLSSHSPGSGS -> IPAPTTTKSCRETFLKW (in isoform
6)"
/evidence="ECO:0000303|PubMed:22941036,
ECO:0000303|PubMed:9212228"
/id="VSP_003283"
VAR_SEQ 71..1095
/note="Missing (in isoform 6)"
/evidence="ECO:0000303|PubMed:22941036,
ECO:0000303|PubMed:9212228"
/id="VSP_003284"
VAR_SEQ 88..1139
/note="Missing (in isoform F)"
/evidence="ECO:0000303|Ref.14"
/id="VSP_035047"
VAR_SEQ 97..1255
/note="Missing (in isoform ZD)"
/evidence="ECO:0000303|PubMed:15623537,
ECO:0000303|PubMed:22941036"
/id="VSP_047576"
VAR_SEQ 1077..1181
/note="Missing (in isoform 9 and isoform S2)"
/evidence="ECO:0000303|PubMed:22941036, ECO:0000303|Ref.12,
ECO:0000303|Ref.15"
/id="VSP_003287"
VAR_SEQ 1077..1087
/note="FLQIYKQGGFL -> VSIGLSFPMLP (in isoform 5)"
/evidence="ECO:0000303|PubMed:2351132"
/id="VSP_003288"
VAR_SEQ 1088..1255
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:2351132"
/id="VSP_003289"
VAR_SEQ 1141..1180
/note="VSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIA -> GCLSVPPK
ELRAAGHLSSPGYLPSYERVPHLPHPWALCAP (in isoform M6)"
/evidence="ECO:0000303|PubMed:22941036, ECO:0000303|Ref.16"
/id="VSP_046962"
VAR_SEQ 1181..1255
/note="Missing (in isoform M6)"
/evidence="ECO:0000303|PubMed:22941036, ECO:0000303|Ref.16"
/id="VSP_046963"
VAR_SEQ 1232..1255
/note="VSAGNGGSSLSYTNPAVAATSANL -> RQNGWSTMPRGALPEESQG (in
isoform J13)"
/evidence="ECO:0000303|PubMed:22941036"
/id="VSP_047874"
VARIANT 1117
/note="V -> M (in dbSNP:rs1611770)"
/evidence="ECO:0000269|PubMed:15969018,
ECO:0000269|PubMed:22941036, ECO:0000269|Ref.17"
/id="VAR_019390"
VARIANT 1142
/note="S -> N (in dbSNP:rs11465207)"
/evidence="ECO:0000269|Ref.17"
/id="VAR_019391"
MUTAGEN 1098
/note="S->A,D,E,F,G,H,I,K,L,M,N,P,Q,R,V,W,Y: Completely
abrogates cleavage."
/evidence="ECO:0000269|PubMed:15987679"
MUTAGEN 1098
/note="S->C,T: Almost complete cleavage."
/evidence="ECO:0000269|PubMed:15987679"
MUTAGEN 1116
/note="D->A: Greatly reduced formation of isoform 5/isoform
Y complex."
/evidence="ECO:0000269|PubMed:10197628"
MUTAGEN 1116
/note="D->E: No effect on formation of isoform 5/isoform Y
complex."
/evidence="ECO:0000269|PubMed:10197628"
MUTAGEN 1184
/note="C->A: S-palmitoylation reduced by 50%. Complete loss
of palmitoylation, no effect on endocytosis, recycling
inhibited and AP1S1 binding reduced by 30%; when associated
with C-1186. Accumulates in intracellular compartments;
when associated with C-1186 and N-1203."
/evidence="ECO:0000269|PubMed:16507569"
MUTAGEN 1186
/note="C->A: S-palmitoylation reduced by 50%. Complete loss
of palmitoylation, no effect on endocytosis, recycling
inhibited, and AP1S1 binding reduced by 30%; when
associated with C-1184. Accumulates in intracellular
compartments; when associated with C-1184 and N-1203."
/evidence="ECO:0000269|PubMed:16507569"
MUTAGEN 1187..1189
/note="RRK->AAA: No nuclear targeting of HRG-stimulated
MUC1 C-terminal nor JUP/gamma-catenin. No effect on
interaction with JUP/gamma-catenin."
/evidence="ECO:0000269|PubMed:12939402,
ECO:0000269|PubMed:16507569"
MUTAGEN 1187..1189
/note="RRK->QQQ: No effect on palmitoylation."
/evidence="ECO:0000269|PubMed:12939402,
ECO:0000269|PubMed:16507569"
MUTAGEN 1191
/note="Y->F: No effect on EGFR-mediated phosphorylation."
/evidence="ECO:0000269|PubMed:11483589,
ECO:0000269|PubMed:15471854"
MUTAGEN 1191
/note="Y->N: No effect on endocytosis."
/evidence="ECO:0000269|PubMed:11483589,
ECO:0000269|PubMed:15471854"
MUTAGEN 1203
/note="Y->E: No effect on nuclear colocalization of MUC1CT
and CTNNB1. No effect on in vitro PDFGR-induced cell
invasiveness."
/evidence="ECO:0000269|PubMed:11483589,
ECO:0000269|PubMed:15471854, ECO:0000269|PubMed:16507569,
ECO:0000269|PubMed:17545600"
MUTAGEN 1203
/note="Y->F: No effect on EGFR-mediated phosphorylation. No
nuclear localization of MUC1CT. Reduced in vitro PDGFR-
induced cell invasiveness."
/evidence="ECO:0000269|PubMed:11483589,
ECO:0000269|PubMed:15471854, ECO:0000269|PubMed:16507569,
ECO:0000269|PubMed:17545600"
MUTAGEN 1203
/note="Y->N: Reduced endocytosis by 30%. Greatly reduced
binding to AP1S2 and GRB2. Binding AP1S1 reduced by 25%.
Reduced endocytosis by 77%; when associated with N-1243.
Accumulates in intracellular compartments; when associated
with C-1184 and C-1186."
/evidence="ECO:0000269|PubMed:11483589,
ECO:0000269|PubMed:15471854, ECO:0000269|PubMed:16507569,
ECO:0000269|PubMed:17545600"
MUTAGEN 1209
/note="Y->F: Some reduction in EGFR-mediated
phosphorylation."
/evidence="ECO:0000269|PubMed:11483589"
MUTAGEN 1218
/note="Y->F: No effect on EGFR-mediated phosphorylation. No
nuclear colocalization of MUC1CT and CTNNB1."
/evidence="ECO:0000269|PubMed:11483589,
ECO:0000269|PubMed:17545600"
MUTAGEN 1223
/note="S->A: No change in PRKCD- nor GSK3B-mediated
phosphorylation."
/evidence="ECO:0000269|PubMed:11877440,
ECO:0000269|PubMed:9819408"
MUTAGEN 1224
/note="T->A: Loss of PRKCD-mediated phosphorylation.
Decreased PRKCD binding. No increased binding to CTNNB1 in
the presence of autophosphorylated PRKCD. Increases
formation of E-cadherin/beta-catenin complex."
/evidence="ECO:0000269|PubMed:11877440"
MUTAGEN 1227
/note="S->A: No change in PRKCD-mediated phosphorylation.
Loss of GSK3B-mediated phosphorylation. CTNNB1."
/evidence="ECO:0000269|PubMed:11877440,
ECO:0000269|PubMed:9819408"
MUTAGEN 1229
/note="Y->F: Greatly reduced EGFR- and Src-mediated
phosphorylation. No nuclear localization of MUC1CT. Reduced
in vitro PDGFR-mediated phosphorylation. Decreased Src-
binding."
/evidence="ECO:0000269|PubMed:11152665,
ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:14688481,
ECO:0000269|PubMed:15471854"
MUTAGEN 1229
/note="Y->N: No effect on endocytosis."
/evidence="ECO:0000269|PubMed:11152665,
ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:14688481,
ECO:0000269|PubMed:15471854"
MUTAGEN 1243
/note="Y->N: Reduces binding to AP1S2 by 33%. Greatly
reduced binding to GRB2. Reduced endocytosis by 50%.
Reduced endocytosis by 77%; when associated with N-1203."
/evidence="ECO:0000269|PubMed:15471854"
CONFLICT 2
/note="T -> A (in Ref. 24; AAD14369)"
/evidence="ECO:0000305"
CONFLICT 134
/note="P -> Q (in Ref. 22; AAA35757)"
/evidence="ECO:0000305"
CONFLICT 154
/note="P -> Q (in Ref. 22; AAA35757)"
/evidence="ECO:0000305"
CONFLICT 1021
/note="S -> T (in Ref. 2; AAA35805/AAA35807 and 3;
AAA59876)"
/evidence="ECO:0000305"
CONFLICT 1143
/note="D -> G (in Ref. 11; AAP97018)"
/evidence="ECO:0000305"
CONFLICT 1193
/note="Q -> L (in Ref. 13; AAK30142)"
/evidence="ECO:0000305"
CONFLICT 1231
/note="K -> T (in Ref. 9; AAD10858)"
/evidence="ECO:0000305"
CONFLICT 1251
/note="T -> A (in Ref. 1; AAA60019)"
/evidence="ECO:0000305"
STRAND 1042..1052
/evidence="ECO:0007744|PDB:2ACM"
HELIX 1056..1059
/evidence="ECO:0007744|PDB:2ACM"
HELIX 1064..1080
/evidence="ECO:0007744|PDB:2ACM"
TURN 1082..1085
/evidence="ECO:0007744|PDB:2ACM"
STRAND 1086..1096
/evidence="ECO:0007744|PDB:2ACM"
STRAND 1099..1107
/evidence="ECO:0007744|PDB:2ACM"
TURN 1109..1111
/evidence="ECO:0007744|PDB:2ACM"
HELIX 1114..1132
/evidence="ECO:0007744|PDB:2ACM"
STRAND 1136..1142
/evidence="ECO:0007744|PDB:2ACM"
SEQUENCE 1255 AA; 122102 MW; 5E28DFC4C20D9A82 CRC64;
MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNAVSMTSSV
LSSHSPGSGS STTQGQDVTL APATEPASGS AATWGQDVTS VPVTRPALGS TTPPAHDVTS
APDNKPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDNRPALGS TAPPVHNVTS
ASGSASGSAS TLVHNGTSAR ATTTPASKST PFSIPSHHSD TPTTLASHST KTDASSTHHS
SVPPLTSSNH STSPQLSTGV SFFFLSFHIS NLQFNSSLED PSTDYYQELQ RDISEMFLQI
YKQGGFLGLS NIKFRPGSVV VQLTLAFREG TINVHDVETQ FNQYKTEAAS RYNLTISDVS
VSDVPFPFSA QSGAGVPGWG IALLVLVCVL VALAIVYLIA LAVCQCRRKN YGQLDIFPAR
DTYHPMSEYP TYHTHGRYVP PSSTDRSPYE KVSAGNGGSS LSYTNPAVAA TSANL


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