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P15941 (MUC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mucin-1

Short name=MUC-1
Alternative name(s):
Breast carcinoma-associated antigen DF3
Cancer antigen 15-3
Short name=CA 15-3
Carcinoma-associated mucin
Episialin
H23AG
Krebs von den Lungen-6
Short name=KL-6
PEMT
Peanut-reactive urinary mucin
Short name=PUM
Polymorphic epithelial mucin
Short name=PEM
Tumor-associated epithelial membrane antigen
Short name=EMA
Tumor-associated mucin
CD_antigen=CD227

Cleaved into the following 2 chains:

  1. Mucin-1 subunit alpha
    Short name=MUC1-NT
    Short name=MUC1-alpha
  2. Mucin-1 subunit beta
    Short name=MUC1-beta
    Alternative name(s):
    MUC1-CT
Gene names
Name:MUC1
Synonyms:PUM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.32 Ref.43 Ref.46 Ref.51 Ref.52 Ref.55 Ref.58 Ref.59 Ref.61

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. Ref.32 Ref.43 Ref.46 Ref.51 Ref.52 Ref.55 Ref.58 Ref.59 Ref.61

Subunit structure

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. Ref.30 Ref.32 Ref.36 Ref.38 Ref.40 Ref.42 Ref.43 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.61

Subcellular location

Apical cell membrane; Single-pass type I membrane protein. 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. Ref.39 Ref.48 Ref.49 Ref.50 Ref.54 Ref.56 Ref.58 Ref.60

Isoform 5: Secreted Ref.39 Ref.48 Ref.49 Ref.50 Ref.54 Ref.56 Ref.58 Ref.60.

Isoform Y: Secreted Ref.39 Ref.48 Ref.49 Ref.50 Ref.54 Ref.56 Ref.58 Ref.60.

Isoform 9: Secreted Ref.39 Ref.48 Ref.49 Ref.50 Ref.54 Ref.56 Ref.58 Ref.60.

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. Ref.39 Ref.48 Ref.49 Ref.50 Ref.54 Ref.56 Ref.58 Ref.60

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 7is expressed in tumor cells only. Ref.9 Ref.55

Developmental stage

During fetal development, expressed at low levels in the colonic epithelium from 13 weeks of gestation. Ref.34

Post-translational modification

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. Ref.28 Ref.31 Ref.33 Ref.35 Ref.54 Ref.64

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/Xbut not on isoform MUC1/Y Ectodomain shedding is mediated by ADAM17.

Dual palmitoylation on cysteine residues in the CQC motif is required for recycling from endosomes back to the plasma membrane. Ref.56

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. Ref.29 Ref.30 Ref.36 Ref.40 Ref.42 Ref.43 Ref.44 Ref.45 Ref.52 Ref.55 Ref.60

The N-terminal sequence has been shown to begin at position 24 or 28 (Ref.26).

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.

Involvement in disease

MUC1/CA 15-3 is used as a serological clinical marker of breast cancer to monitor response to breast cancer treatment and disease recurrence (Ref.62). 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.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.63

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.

Sequence similarities

Contains 1 SEA domain.

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 (Ref.31, Ref.35).

Sequence caution

The sequence AAD14369.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAD14376.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   PTMAutocatalytic cleavage
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Inferred from direct assay Ref.51. Source: BHF-UCL

DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from direct assay Ref.51. Source: BHF-UCL

O-glycan processing

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from direct assay Ref.51. Source: BHF-UCL

negative regulation of transcription by competitive promoter binding

Inferred from direct assay Ref.51. Source: BHF-UCL

positive regulation of histone H4 acetylation

Inferred from direct assay Ref.51. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter in response to stress

Inferred from direct assay Ref.51. Source: BHF-UCL

post-translational protein modification

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase II promoter in response to stress

Inferred from direct assay Ref.51. Source: BHF-UCL

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

apical plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell surface

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289PubMed 19056867PubMed 19199708. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.3. Source: ProtInc

nuclear chromatin

Inferred from direct assay Ref.51. Source: BHF-UCL

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay Ref.51. Source: BHF-UCL

p53 binding

Inferred from physical interaction Ref.51. Source: BHF-UCL

transcription cofactor activity

Inferred from direct assay Ref.51. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 17 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P15941-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P15941-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: T → TATTAPKPAT
Isoform 3 (identifier: P15941-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     19-21: Missing.
Isoform 4 (identifier: P15941-4)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     20-31: Missing.
Isoform 5 (identifier: P15941-5)

Also known as: SEC;

The sequence of this isoform differs from the canonical sequence as follows:
     1077-1087: FLQIYKQGGFL → VSIGLSFPMLP
     1088-1255: Missing.
Isoform 6 (identifier: P15941-6)

Also known as: X;

The sequence of this isoform differs from the canonical sequence as follows:
     54-70: VSMTSSVLSSHSPGSGS → IPAPTTTKSCRETFLKW
     71-1095: Missing.
Isoform Y (identifier: P15941-7)

Also known as: MUC1/Y;

The sequence of this isoform differs from the canonical sequence as follows:
     54-1053: Missing.
Isoform 8 (identifier: P15941-8)

Also known as: Z;

The sequence of this isoform differs from the canonical sequence as follows:
     54-1035: Missing.
Isoform 9 (identifier: P15941-9)

Also known as: S;

The sequence of this isoform differs from the canonical sequence as follows:
     54-1035: Missing.
     1077-1181: Missing.
Isoform F (identifier: P15941-10)

The sequence of this isoform differs from the canonical sequence as follows:
     54-87: VSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPA → IPAPTTTKSCRETFLKCFCRFINKGVFWASPILS
     88-1139: Missing.
Isoform Y-LSP (identifier: P15941-11)

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: T → TATTAPKPAT
     54-1053: Missing.
Note: Lacks the mucin repeats.
Isoform S2 (identifier: P15941-12)

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: T → TATTAPKPAT
     54-1053: Missing.
     1077-1181: Missing.
Isoform M6 (identifier: P15941-13)

The sequence of this isoform differs from the canonical sequence as follows:
     54-1035: Missing.
     1141-1180: VSDVPFPFSA...VALAIVYLIA → GCLSVPPKEL...LPHPWALCAP
     1181-1255: Missing.
Isoform ZD (identifier: P15941-14)

Also known as: J19;

The sequence of this isoform differs from the canonical sequence as follows:
     54-96: VSMTSSVLSS...ASGSAATWGQ → IPAPTTTKSC...SSGQDLWWYN
     97-1255: Missing.
Note: Lacks the mucin repeats. Exists as a disulfide-linked oligomer.
Isoform T10 (identifier: P15941-15)

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: T → TATTAPKPAT
     54-1093: Missing.
Isoform E2 (identifier: P15941-16)

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: T → TATTAPKPAT
     54-1151: Missing.
Isoform J13 (identifier: P15941-17)

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: T → TATTAPKPAT
     54-1053: Missing.
     1232-1255: VSAGNGGSSLSYTNPAVAATSANL → RQNGWSTMPRGALPEESQG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.26
Chain24 – 12551232Mucin-1
PRO_0000019277
Chain24 – 10971074Mucin-1 subunit alpha
PRO_0000317446
Chain1098 – 1255158Mucin-1 subunit beta
PRO_0000317447

Regions

Topological domain24 – 11581135Extracellular Potential
Transmembrane1159 – 118123Helical; Potential
Topological domain1182 – 125574Cytoplasmic Potential
Repeat61 – 80201; approximate
Repeat81 – 100202; approximate
Repeat101 – 120203
Repeat121 – 140204
Repeat141 – 160205
Repeat161 – 180206
Repeat181 – 200207
Repeat201 – 220208
Repeat221 – 240209
Repeat241 – 2602010
Repeat261 – 2802011
Repeat281 – 3002012
Repeat301 – 3202013
Repeat321 – 3402014
Repeat341 – 3602015
Repeat361 – 3802016
Repeat381 – 4002017
Repeat401 – 4202018
Repeat421 – 4402019
Repeat441 – 4602020
Repeat461 – 4802021
Repeat481 – 5002022
Repeat501 – 5202023
Repeat521 – 5402024
Repeat541 – 5602025
Repeat561 – 5802026
Repeat581 – 6002027
Repeat601 – 6202028
Repeat621 – 6402029
Repeat641 – 6602030
Repeat661 – 6802031
Repeat681 – 7002032
Repeat701 – 7202033
Repeat721 – 7402034
Repeat741 – 7602035
Repeat761 – 7802036
Repeat781 – 8002037
Repeat801 – 8202038
Repeat821 – 8402039
Repeat841 – 8602040
Repeat861 – 8802041
Repeat881 – 9002042
Repeat901 – 9202043
Repeat921 – 9402044
Repeat941 – 9602045
Repeat961 – 9802046; approximate
Repeat981 – 10002047; approximate
Repeat1001 – 10202048; approximate
Domain1039 – 1148110SEA
Region126 – 96584042 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
Region1192 – 122837Interaction with P53
Region1223 – 12308Required for interaction with GSK3B
Region1233 – 12419Required for interaction with beta- and gamma-catenins
Motif1203 – 12064Interaction with GRB2
Motif1229 – 12324Interaction with SRC and ESR1
Motif1243 – 12464Required for interaction with AP1S2

Sites

Site1097 – 10982Cleavage; by autolysis

Amino acid modifications

Modified residue11911Phosphotyrosine
Modified residue12031Phosphotyrosine; by PDGFR Ref.44 Ref.60
Modified residue12091Phosphotyrosine
Modified residue12121Phosphotyrosine Ref.44
Modified residue12181Phosphotyrosine; by PDGFR Ref.60
Modified residue12241Phosphothreonine; by PKC/PRKCD Ref.43
Modified residue12271Phosphoserine; by GSK3-beta Ref.36
Modified residue12291Phosphotyrosine; by CSK, EGFR and SRC Ref.40 Ref.42 Ref.44 Ref.60
Modified residue12431Phosphotyrosine Ref.44
Lipidation11841S-palmitoyl cysteine Ref.56
Lipidation11861S-palmitoyl cysteine Ref.56
Glycosylation1311O-linked (GalNAc...) Probable
Glycosylation1391O-linked (GalNAc...) Probable
Glycosylation1401O-linked (GalNAc...) Potential
Glycosylation1441O-linked (GalNAc...) Potential
Glycosylation9571N-linked (GlcNAc...) Potential
Glycosylation9751N-linked (GlcNAc...) Potential
Glycosylation10291N-linked (GlcNAc...) Potential
Glycosylation10551N-linked (GlcNAc...) Potential
Glycosylation11331N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence19 – 213Missing in isoform 3.
VSP_003281
Alternative sequence191T → TATTAPKPAT in isoform 2, isoform Y-LSP, isoform E2, isoform J13, isoform S2 and isoform T10.
VSP_003280
Alternative sequence20 – 3112Missing in isoform 4.
VSP_003282
Alternative sequence54 – 11511098Missing in isoform E2.
VSP_047872
Alternative sequence54 – 10931040Missing in isoform T10.
VSP_047873
Alternative sequence54 – 10531000Missing in isoform J13, isoform Y, isoform Y-LSP and isoform S2.
VSP_003285
Alternative sequence54 – 1035982Missing in isoform 8, isoform 9 and isoform M6.
VSP_003286
Alternative sequence54 – 9643VSMTS…ATWGQ → IPAPTTTKSCRETFLKCFCR FINKGVFWASPILSSGQDLW WYN in isoform ZD.
VSP_047575
Alternative sequence54 – 8734VSMTS…ATEPA → IPAPTTTKSCRETFLKCFCR FINKGVFWASPILS in isoform F.
VSP_035046
Alternative sequence54 – 7017VSMTS…PGSGS → IPAPTTTKSCRETFLKW in isoform 6.
VSP_003283
Alternative sequence71 – 10951025Missing in isoform 6.
VSP_003284
Alternative sequence88 – 11391052Missing in isoform F.
VSP_035047
Alternative sequence97 – 12551159Missing in isoform ZD.
VSP_047576
Alternative sequence1077 – 1181105Missing in isoform 9 and isoform S2.
VSP_003287
Alternative sequence1077 – 108711FLQIYKQGGFL → VSIGLSFPMLP in isoform 5.
VSP_003288
Alternative sequence1088 – 1255168Missing in isoform 5.
VSP_003289
Alternative sequence1141 – 118040VSDVP…VYLIA → GCLSVPPKELRAAGHLSSPG YLPSYERVPHLPHPWALCAP in isoform M6.
VSP_046962
Alternative sequence1181 – 125575Missing in isoform M6.
VSP_046963
Alternative sequence1232 – 125524VSAGN…TSANL → RQNGWSTMPRGALPEESQG in isoform J13.
VSP_047874
Natural variant11171V → M. Ref.11 Ref.13 Ref.17
Corresponds to variant rs1611770 [ dbSNP | Ensembl ].
VAR_019390
Natural variant11421S → N. Ref.17
Corresponds to variant rs11465207 [ dbSNP | Ensembl ].
VAR_019391

Experimental info

Mutagenesis10981S → A, D, E, F, G, H, I, K, L, M, N, P, Q, R, V, W or Y: Completely abrogates cleavage. Ref.27
Mutagenesis10981S → C or T: Almost complete cleavage. Ref.27
Mutagenesis11161D → A: Greatly reduced formation of isoform 5/isoform Y complex. Ref.37
Mutagenesis11161D → E: No effect on formation of isoform 5/isoform Y complex. Ref.37
Mutagenesis11841C → 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. Ref.56
Mutagenesis11861C → 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. Ref.56
Mutagenesis1187 – 11893RRK → AAA: No nuclear targeting of HRG-stimulated MUC1 C-terminal nor JUP/gamma-catenin. No effect on interaction with JUP/gamma-catenin. Ref.49 Ref.56
Mutagenesis1187 – 11893RRK → QQQ: No effect on palmitoylation. Ref.49 Ref.56
Mutagenesis11911Y → F: No effect on EGFR-mediated phosphorylation. Ref.42 Ref.50
Mutagenesis11911Y → N: No effect on endocytosis. Ref.42 Ref.50
Mutagenesis12031Y → E: No effect on nuclear colocalization of MUC1CT and CTNNB1. No effect on in vitro PDFGR-induced cell invasiveness. Ref.42 Ref.50 Ref.56 Ref.60
Mutagenesis12031Y → F: No effect on EGFR-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-induced cell invasiveness. Ref.42 Ref.50 Ref.56 Ref.60
Mutagenesis12031Y → 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. Ref.42 Ref.50 Ref.56 Ref.60
Mutagenesis12091Y → F: Some reduction in EGFR-mediated phosphorylation. Ref.42
Mutagenesis12181Y → F: No effect on EGFR-mediated phosphorylation. No nuclear colocalization of MUC1CT and CTNNB1. Ref.42 Ref.60
Mutagenesis12231S → A: No change in PRKCD- nor GSK3B-mediated phosphorylation. Ref.36 Ref.43
Mutagenesis12241T → 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. Ref.43
Mutagenesis12271S → A: No change in PRKCD-mediated phosphorylation. Loss of GSK3B-mediated phosphorylation. CTNNB1. Ref.36 Ref.43
Mutagenesis12291Y → F: Greatly reduced EGFR- and Src-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-mediated phosphorylation. Decreased Src-binding. Ref.40 Ref.42 Ref.46 Ref.50
Mutagenesis12291Y → N: No effect on endocytosis. Ref.40 Ref.42 Ref.46 Ref.50
Mutagenesis12431Y → 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. Ref.50
Sequence conflict21T → A in AAD14369. Ref.24
Sequence conflict1341P → Q in AAA35757. Ref.22
Sequence conflict1541P → Q in AAA35757. Ref.22
Sequence conflict10211S → T in AAA35805. Ref.2
Sequence conflict10211S → T in AAA35807. Ref.2
Sequence conflict10211S → T in AAA59876. Ref.3
Sequence conflict11431D → G in AAP97018. Ref.11
Sequence conflict11931Q → L in AAK30142. Ref.13
Sequence conflict12311K → T in AAD10858. Ref.9
Sequence conflict12511T → A in AAA60019. Ref.1

Secondary structure

.................. 1255
Helix Strand Turn

Details...

Sequences

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

Last modified May 18, 2010. Version 3.
Checksum: 5E28DFC4C20D9A82

FASTA1,255122,102
        10         20         30         40         50         60 
MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNAVSMTSSV 

        70         80         90        100        110        120 
LSSHSPGSGS STTQGQDVTL APATEPASGS AATWGQDVTS VPVTRPALGS TTPPAHDVTS 

       130        140        150        160        170        180 
APDNKPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       190        200        210        220        230        240 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       250        260        270        280        290        300 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       310        320        330        340        350        360 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       370        380        390        400        410        420 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       430        440        450        460        470        480 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       490        500        510        520        530        540 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       550        560        570        580        590        600 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       610        620        630        640        650        660 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       670        680        690        700        710        720 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       730        740        750        760        770        780 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       790        800        810        820        830        840 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       850        860        870        880        890        900 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 

       910        920        930        940        950        960 
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDNRPALGS TAPPVHNVTS 

       970        980        990       1000       1010       1020 
ASGSASGSAS TLVHNGTSAR ATTTPASKST PFSIPSHHSD TPTTLASHST KTDASSTHHS 

      1030       1040       1050       1060       1070       1080 
SVPPLTSSNH STSPQLSTGV SFFFLSFHIS NLQFNSSLED PSTDYYQELQ RDISEMFLQI 

      1090       1100       1110       1120       1130       1140 
YKQGGFLGLS NIKFRPGSVV VQLTLAFREG TINVHDVETQ FNQYKTEAAS RYNLTISDVS 

      1150       1160       1170       1180       1190       1200 
VSDVPFPFSA QSGAGVPGWG IALLVLVCVL VALAIVYLIA LAVCQCRRKN YGQLDIFPAR 

      1210       1220       1230       1240       1250 
DTYHPMSEYP TYHTHGRYVP PSSTDRSPYE KVSAGNGGSS LSYTNPAVAA TSANL 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 3810149471D221FD
Show »

FASTA1,264122,941
Isoform 3 (C) [UniParc].

Checksum: A3F30DBFE56DD0C5
Show »

FASTA1,252121,803
Isoform 4 (D) [UniParc].

Checksum: B2C6288C94AABC14
Show »

FASTA1,243121,021
Isoform 5 (SEC) [UniParc].

Checksum: 6039CBB69974EA3E
Show »

FASTA1,087103,836
Isoform 6 (X) [UniParc].

Checksum: 53B036250EC1242D
Show »

FASTA23024,566
Isoform Y (MUC1/Y) [UniParc].

Checksum: 46DC2580CF357BEF
Show »

FASTA25527,566
Isoform 8 (Z) [UniParc].

Checksum: B72F7F4FC2D23BCC
Show »

FASTA27329,592
Isoform 9 (S) [UniParc].

Checksum: 53C6544C2B077B89
Show »

FASTA16818,277
Isoform F [UniParc].

Checksum: CC2BE70F8C1B325E
Show »

FASTA20321,556
Isoform Y-LSP [UniParc].

Checksum: 6E192550756A6D4A
Show »

FASTA26428,405
Isoform S2 [UniParc].

Checksum: 2C3B69F515D73168
Show »

FASTA15917,090
Isoform M6 [UniParc].

Checksum: 5300166458B017CB
Show »

FASTA19821,663
Isoform ZD (J19) [UniParc].

Checksum: F2140812C4C11983
Show »

FASTA9610,403
Isoform T10 [UniParc].

Checksum: 977E7703C14AC936
Show »

FASTA22423,747
Isoform E2 [UniParc].

Checksum: BF6C969984986AD0
Show »

FASTA16617,287
Isoform J13 [UniParc].

Checksum: FD53C9223E24B094
Show »

FASTA25928,297

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a human pancreatic tumor mucin cDNA."
Lan M.S., Batra S.K., Qi W.-N., Metzgar R.S., Hollingsworth M.A.
J. Biol. Chem. 265:15294-15299(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Pancreatic carcinoma.
[2]"Episialin, a carcinoma-associated mucin, is generated by a polymorphic gene encoding splice variants with alternative amino termini."
Ligtenberg M.J.L., Vos H.L., Gennissen A.M.C., Hilkens J.
J. Biol. Chem. 265:5573-5578(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"Molecular cloning and expression of human tumor-associated polymorphic epithelial mucin."
Gendler S.J., Lancaster C.A., Taylor-Papadimitriou J., Duhig T., Peat N., Burchell J., Pemberton L., Lalani E.-N., Wilson D.
J. Biol. Chem. 265:15286-15293(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Mammary carcinoma.
[4]"Structure and expression of the human polymorphic epithelial mucin gene: an expressed VNTR unit."
Lancaster C.A., Peat N., Duhig T., Wilson D., Taylor-Papadimitriou J., Gendler S.J.
Biochem. Biophys. Res. Commun. 173:1019-1029(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]"Human epithelial tumor antigen cDNA sequences. Differential splicing may generate multiple protein forms."
Wreschner D.H., Hareuveni M., Tsarfaty I., Smorodinsky N., Horev J., Zaretsky J., Kotkes P., Weiss M., Lathe R., Dion A., Keydar I.
Eur. J. Biochem. 189:463-473(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Tissue: Mammary carcinoma.
[6]"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."
Hareuveni M., Tsarfaty I., Zaretsky J., Kotkes P., Horev J., Zrihan S., Weiss M., Green S., Lathe R., Keydar I., Wreschner D.H.
Eur. J. Biochem. 189:475-486(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[7]"Isolation and characterization of an expressed hypervariable gene coding for a breast-cancer-associated antigen."
Tsarfaty I., Hareuveni M., Horev J., Zaretsky J., Weiss M., Jeltsch J.-M., Garnier J.-M., Lathe R., Keydar I., Wreschner D.H.
Gene 93:313-318(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[8]"Characterization and molecular cloning of a novel MUC1 protein, devoid of tandem repeats, expressed in human breast cancer tissue."
Zrihan-Licht S., Vos H.L., Baruch A., Elroy-Stein O., Sagiv D., Keydar I., Hilkens J., Wreschner D.H.
Eur. J. Biochem. 224:787-795(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM Y).
[9]"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)."
Oosterkamp H.M., Scheiner L., Stefanova M.C., Lloyd K.O., Finstad C.L.
Int. J. Cancer 72:87-94(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; Y AND 8), TISSUE SPECIFICITY.
[10]"A novel protein derived from the MUC1 gene by alternative splicing and frameshifting."
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.
J. Biol. Chem. 280:10655-10663(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZD).
[11]"Human mucin MUC1 RNA undergoes different types of alternative splicing resulting in multiple isoforms."
Zhang L., Vlad A., Milcarek C., Finn O.J.
Cancer Immunol. Immunother. 62:423-435(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; E2; J13; M6; S2; T10; Y-LSP AND ZD), ALTERNATIVE SPLICING, VARIANT MET-1117.
[12]"Cloning of a new potential secreted short variant form of MUC1 mucin in epithelial cancer cell line."
Zhang L.X., Li C.H., Sun L.Y., Yue W.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
Tissue: Carcinoma.
[13]"Soluble expression of peptide containing MUC1/Y-specific epitope in Escherichia coli and preparation of the antibody."
Zhang L.X., Li C.H., Sun L.Y., Wang M., Lu H.J.
Sheng Wu Gong Cheng Xue Bao 19:337-342(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM Y), VARIANT MET-1117.
Tissue: Cervix carcinoma.
[14]"Cloning of a new MUC1 short variant mRNA F from HeLa cells."
Zhang L.X., Lu H.J.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F).
[15]"Cloning of a new MUC1 short variant mRNA S2 from HeLa cells."
Zhang L.X., Lu H.J.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S2).
[16]"Isolation of MUC1 isoforms from MCF7 cells."
Zhang L., Finn O.J.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M6).
[17]NIEHS SNPs program
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-1117 AND ASN-1142.
[18]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[19]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[20]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS Y AND Y-LSP).
[21]"A highly immunogenic region of a human polymorphic epithelial mucin expressed by carcinomas is made up of tandem repeats."
Gendler S.J., Taylor-Papadimitriou J., Duhig T., Rothbard J., Burchell J.
J. Biol. Chem. 263:12820-12823(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[22]"Sequence analysis of the 5' region of the human DF3 breast carcinoma-associated antigen gene."
Abe M., Siddiqui J., Kufe D.
Biochem. Biophys. Res. Commun. 165:644-649(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-160 (ISOFORM 2).
[23]"Preoperative diagnosis of thyroid papillary carcinoma by reverse transcriptase polymerase chain reaction of the MUC1 gene."
Weiss M., Baruch A., Keydar I., Wreschner D.H.
Int. J. Cancer 66:55-59(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-109 (ISOFORM 2).
Tissue: Thyroid.
[24]"Mucin mRNA expression in lung adenocarcinoma cell lines and tissues."
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.
Oncology 53:118-126(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-89.
Tissue: Lung.
[25]Buluwela L., Liu Q., Luqmani Y.A., Gomm J.J., Coombes R.C.
Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-46 (ISOFORMS 3 AND 4).
Tissue: Mammary carcinoma.
[26]"Identification of MUC1 proteolytic cleavage sites in vivo."
Parry S., Silverman H.S., McDermott K., Willis A., Hollingsworth M.A., Harris A.
Biochem. Biophys. Res. Commun. 283:715-720(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-33; 28-37 AND 1098-1107, PROTEOLYTIC PROCESSING.
[27]"The MUC1 SEA module is a self-cleaving domain."
Levitin F., Stern O., Weiss M., Gil-Henn C., Ziv R., Prokocimer Z., Smorodinsky N.I., Rubinstein D.B., Wreschner D.H.
J. Biol. Chem. 280:33374-33386(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1098-1111, PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF SER-1098.
[28]"High density O-glycosylation on tandem repeat peptide from secretory MUC1 of T47D breast cancer cells."
Mueller S., Alving K., Peter-Katalinic J., Zachara N., Gooley A.A., Hanisch F.-G.
J. Biol. Chem. 274:18165-18172(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF TANDEM REPEAT, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION.
[29]"Tyrosine phosphorylation of the MUC1 breast cancer membrane proteins. Cytokine receptor-like molecules."
Zrihan-Licht S., Baruch A., Elroy-Stein O., Keydar I., Wreschner D.H.
FEBS Lett. 356:130-136(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[30]"Association of the DF3/MUC1 breast cancer antigen with Grb2 and the Sos/Ras exchange protein."
Pandey P., Kharbanda S., Kufe D.
Cancer Res. 55:4000-4003(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH SOS1 AND GRB2, INTERACTION WITH GRB2 AND SOS1, PHOSPHORYLATION.
[31]"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."
Stadie T.R., Chai W., Lawson A.M., Byfield P.G., Hanisch F.G.
Eur. J. Biochem. 229:140-147(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-131 AND THR-139, IDENTIFICATION BY MASS SPECTROMETRY.
[32]"Interaction of the DF3/MUC1 breast carcinoma-associated antigen and beta-catenin in cell adhesion."
Yamamoto M., Bharti A., Li Y., Kufe D.
J. Biol. Chem. 272:12492-12494(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNB1 AND JUP, FUNCTION.
[33]"Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo."
Mueller S., Goletz S., Packer N.H., Gooley A.A., Lawson A.M., Hanisch F.-G.
J. Biol. Chem. 272:24780-24793(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION WITHIN TANDEM REPEAT.
[34]"Developmental expression of mucin genes in the human gastrointestinal system."
Reid C.J., Harris A.
Gut 42:220-226(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[35]"Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry."
Hanisch F.G., Green B.N., Bateman R., Peter-Katalinic J.
J. Mass Spectrom. 33:358-362(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-131 AND THR-139, IDENTIFICATION BY MASS SPECTROMETRY.
[36]"Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-associated antigen and beta-catenin."
Li Y., Bharti A., Chen D., Gong J., Kufe D.
Mol. Cell. Biol. 18:7216-7224(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GSK3B AND CTNNB1, PHOSPHORYLATION AT SER-1227, MUTAGENESIS OF SER-1223 AND SER-1227.
[37]"The breast cancer-associated MUC1 gene generates both a receptor and its cognate binding protein."
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.
Cancer Res. 59:1552-1561(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION (ISOFORM Y), MUTAGENESIS OF ASP-1116.
[38]"MUC1 mucin core protein binds to the domain 1 of ICAM-1."
Hayashi T., Takahashi T., Motoya S., Ishida T., Itoh F., Adachi M., Hinoda Y., Imai K.
Digestion 63 Suppl. 1:87-92(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ICAM1.
[39]"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."
Bennett R. Jr., Jaervelae T., Engelhardt P., Kostamovaara L., Sparks P., Carpen O., Turunen O., Vaheri A.
J. Histochem. Cytochem. 49:67-77(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[40]"The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 beta and beta-catenin."
Li Y., Kuwahara H., Ren J., Wen G., Kufe D.
J. Biol. Chem. 276:6061-6064(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRC; GSK3B AND CTNNB1, PHOSPHORYLATION AT TYR-1229, MUTAGENESIS OF TYR-1229.
[41]"Identification and topology of variant sequences within individual repeat domains of the human epithelial tumor mucin MUC1."
Engelmann K., Baldus S.E., Hanisch F.-G.
J. Biol. Chem. 276:27764-27769(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM WITHIN THE REPEAT.
[42]"The epidermal growth factor receptor regulates interaction of the human DF3/MUC1 carcinoma antigen with c-Src and beta-catenin."
Li Y., Ren J., Yu W., Li Q., Kuwahara H., Yin L., Carraway K.L. III, Kufe D.
J. Biol. Chem. 276:35239-35242(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EGFR, PHOSPHORYLATION AT TYR-1229 BY EGFR, MUTAGENESIS OF TYR-1191; TYR-1203; TYR-1209; TYR-1218 AND TYR-1229.
[43]"Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in beta-catenin signaling."
Ren J., Li Y., Kufe D.
J. Biol. Chem. 277:17616-17622(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-1224, INTERACTION WITH PRKCD, FUNCTION, MUTAGENESIS OF SER-1223; THR-1224 AND SER-1227.
[44]"Identification of four sites of stimulated tyrosine phosphorylation in the MUC1 cytoplasmic tail."
Wang H., Lillehoj E.P., Kim K.C.
Biochem. Biophys. Res. Commun. 310:341-346(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-1203; TYR-1212; TYR-1229 AND TYR-1243.
[45]"DF3/MUC1 signaling in multiple myeloma cells is regulated by interleukin-7."
Li Y., Chen W., Ren J., Yu W.H., Li Q., Yoshida K., Kufe D.
Cancer Biol. Ther. 2:187-193(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LYN, PHOSPHORYLATION.
[46]"MUC1 cytoplasmic domain coactivates Wnt target gene transcription and confers transformation."
Huang L., Ren J., Chen D., Li Y., Kharbanda S., Kufe D.
Cancer Biol. Ther. 2:702-706(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNB1, FUNCTION, MUTAGENESIS OF TYR-1229.
[47]"Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1 shedding."
Thathiah A., Blobel C.P., Carson D.D.
J. Biol. Chem. 278:3386-3394(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAM17, CLEAVAGE.
[48]"Nuclear association of the cytoplasmic tail of MUC1 and beta-catenin."
Wen Y., Caffrey T.C., Wheelock M.J., Johnson K.R., Hollingsworth M.A.
J. Biol. Chem. 278:38029-38039(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION.
[49]"Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein."
Li Y., Yu W.-H., Ren J., Chen W., Huang L., Kharbanda S., Loda M., Kufe D.
Mol. Cancer Res. 1:765-775(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB2; ERBB3 AND ERBB4, SUBCELLULAR LOCATION, MUTAGENESIS OF 1187-ARG--LYS-1189.
[50]"MUC1 membrane trafficking is modulated by multiple interactions."
Kinlough C.L., Poland P.A., Bruns J.B., Harkleroad K.L., Hughey R.P.
J. Biol. Chem. 279:53071-53077(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP1S2 AND GRB2, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-1191; TYR-1203; TYR-1229 AND TYR-1243.
[51]"Human MUC1 oncoprotein regulates p53-responsive gene transcription in the genotoxic stress response."
Wei X., Xu H., Kufe D.
Cancer Cell 7:167-178(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53, FUNCTION.
[52]"MUC1 oncoprotein blocks glycogen synthase kinase 3beta-mediated phosphorylation and degradation of beta-catenin."
Huang L., Chen D., Liu D., Yin L., Kharbanda S., Kufe D.
Cancer Res. 65:10413-10422(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GSK3B, PHOSPHORYLATION, FUNCTION.
[53]Erratum
Kinlough C.L., Poland P.A., Bruns J.B., Harkleroad K.L., Hughey R.P.
J. Biol. Chem. 280:28827-28827(2005)
[54]"Transmembrane and secreted MUC1 probes show trafficking-dependent changes in O-glycan core profiles."
Engelmann K., Kinlough C.L., Muller S., Razawi H., Baldus S.E., Hughey R.P., Hanisch F.-G.
Glycobiology 15:1111-1124(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[55]"MUC1 (CD227) interacts with lck tyrosine kinase in Jurkat lymphoma cells and normal T cells."
Mukherjee P., Tinder T.L., Basu G.D., Gendler S.J.
J. Leukoc. Biol. 77:90-99(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LCK, PHOSPHORYLATION, FUNCTION, TISSUE SPECIFICITY.
[56]"Recycling of MUC1 is dependent on its palmitoylation."
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.
J. Biol. Chem. 281:12112-12122(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-1184 AND CYS-1186, SUBCELLULAR LOCATION, INTERACTION WITH AP1S1 AND AP1S2, MUTAGENESIS OF CYS-1184; CYS-1186; TYR-1203 AND 1187-ARG--LYS-1189.
[57]"MUC1 oncoprotein stabilizes and activates estrogen receptor alpha."
Wei X., Xu H., Kufe D.
Mol. Cell 21:295-305(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ESR1.
[58]"MUC1 inhibits cell proliferation by a beta-catenin-dependent mechanism."
Lillehoj E.P., Lu W., Kiser T., Goldblum S.E., Kim K.C.
Biochim. Biophys. Acta 1773:1028-1038(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, FUNCTION.
[59]"Human mucin 1 oncoprotein represses transcription of the p53 tumor suppressor gene."
Wei X., Xu H., Kufe D.
Cancer Res. 67:1853-1858(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLF4, FUNCTION.
[60]"Platelet-derived growth factor receptor beta-mediated phosphorylation of MUC1 enhances invasiveness in pancreatic adenocarcinoma cells."
Singh P.K., Wen Y., Swanson B.J., Shanmugam K., Kazlauskas A., Cerny R.L., Gendler S.J., Hollingsworth M.A.
Cancer Res. 67:5201-5210(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-1203; TYR-1218 AND TYR-1229, MUTAGENESIS OF TYR-1203 AND TYR-1218, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[61]"MUC1 is a novel regulator of ErbB1 receptor trafficking."
Pochampalli M.R., el Bejjani R.M., Schroeder J.A.
Oncogene 26:1693-1701(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EGFR, FUNCTION.
[62]"CA 15-3: uses and limitation as a biomarker for breast cancer."
Duffy M.J., Evoy D., McDermott E.W.
Clin. Chim. Acta 411:1869-1874(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MARKER IN BREAST CANCER.
[63]"Mutations causing medullary cystic kidney disease type 1 lie in a large VNTR in MUC1 missed by massively parallel sequencing."
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. expand/collapse author list , 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.
Nat. Genet. 45:299-303(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MCKD1.
[64]"N-glycosylation of the MUC1 mucin in epithelial cells and secretions."
Parry S., Hanisch F.G., Leir S.H., Sutton-Smith M., Morris H.R., Dell A., Harris A.
Glycobiology 16:623-634(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1041-1097 AND 1098-1152 OF WILD TYPE AND MUTANT ALA-1098, IDENTIFICATION BY MASS SPECTROMETRY, STRUCTURE OF CARBOHYDRATES, AUTOCATALYTIC CLEAVAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05582 mRNA. Translation: AAA60019.1.
M32738 mRNA. Translation: AAA35804.1.
M32739 mRNA. Translation: AAA35806.1.
M34089 mRNA. Translation: AAA35807.1.
M34088 mRNA. Translation: AAA35805.1.
J05581 mRNA. Translation: AAA59876.1.
M61170 Genomic DNA. Translation: AAB53150.1.
X52229 mRNA. Translation: CAA36478.1. Sequence problems.
X52228 mRNA. Translation: CAA36477.1. Sequence problems.
M35093 Genomic DNA. Translation: AAB59612.1. Sequence problems.
X80761 mRNA. Translation: CAA56734.1.
U60259 mRNA. Translation: AAD10856.1.
U60260 mRNA. Translation: AAD10857.1.
U60261 mRNA. Translation: AAD10858.1.
AF125525 mRNA. Translation: AAD27842.1.
AY466157 mRNA. Translation: AAR28764.1.
AY327582 mRNA. Translation: AAP97013.1.
AY327584 mRNA. Translation: AAP97015.1.
AY327586 mRNA. Translation: AAP97017.1.
AY327587 mRNA. Translation: AAP97018.1.
EF583653 mRNA. Translation: ABQ59628.1.
EF670711 mRNA. Translation: ABS01298.1.
EF670712 mRNA. Translation: ABS01299.1.
FJ226040 mRNA. Translation: ACI25172.1.
FJ226047 mRNA. Translation: ACI25179.1.
AF348143 mRNA. Translation: AAK30142.1.
AY463543 Genomic DNA. Translation: AAR18816.1.
AL713999 Genomic DNA. Translation: CAI95071.1.
AL713999 Genomic DNA. Translation: CAI95073.1.
AL713999 Genomic DNA. Translation: CAI95074.1.
AL713999 Genomic DNA. Translation: CAI95080.1.
CH471121 Genomic DNA. Translation: EAW53116.1.
CH471121 Genomic DNA. Translation: EAW53117.1.
CH471121 Genomic DNA. Translation: EAW53118.1.
CH471121 Genomic DNA. Translation: EAW53119.1.
BC120974 mRNA. Translation: AAI20975.1.
BC120975 mRNA. Translation: AAI20976.1.
Z17324 mRNA. Translation: CAA78972.1.
Z17325 mRNA. Translation: CAA78973.1.
M31823 mRNA. Translation: AAA35757.1.
S81781 mRNA. Translation: AAD14376.1. Different initiation.
S81736 mRNA. Translation: AAD14369.1. Different initiation.
M21868 mRNA. Translation: AAA59874.1. Sequence problems.
PIRA35175.
RefSeqNP_001018016.1. NM_001018016.2.
NP_001018017.1. NM_001018017.2.
NP_001037855.1. NM_001044390.2.
NP_001037856.1. NM_001044391.2.
NP_001037857.1. NM_001044392.2.
NP_001037858.1. NM_001044393.2.
NP_001191214.1. NM_001204285.1.
NP_001191215.1. NM_001204286.1.
NP_001191216.1. NM_001204287.1.
NP_001191217.1. NM_001204288.1.
NP_001191218.1. NM_001204289.1.
NP_001191219.1. NM_001204290.1.
NP_001191220.1. NM_001204291.1.
NP_001191221.1. NM_001204292.1.
NP_001191222.1. NM_001204293.1.
NP_001191223.1. NM_001204294.1.
NP_001191224.1. NM_001204295.1.
NP_001191225.1. NM_001204296.1.
NP_001191226.1. NM_001204297.1.
NP_002447.4. NM_002456.5.
UniGeneHs.89603.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SM3X-ray1.95P919-931[»]
2ACMNMR-A1041-1097[»]
B1098-1152[»]
2FO4X-ray2.70P140-146[»]
ProteinModelPortalP15941.
SMRP15941. Positions 1037-1144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110669. 27 interactions.
DIPDIP-41890N.
IntActP15941. 8 interactions.
MINTMINT-156679.

Protein family/group databases

MEROPSS71.001.

PTM databases

PhosphoSiteP15941.
UniCarbKBP15941.

Polymorphism databases

DMDM296439295.

Proteomic databases

PaxDbP15941.
PRIDEP15941.

Protocols and materials databases

DNASU4582.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337604; ENSP00000338983; ENSG00000185499. [P15941-8]
ENST00000338684; ENSP00000343482; ENSG00000185499. [P15941-15]
ENST00000342482; ENSP00000342814; ENSG00000185499. [P15941-16]
ENST00000343256; ENSP00000339690; ENSG00000185499. [P15941-10]
ENST00000368389; ENSP00000357374; ENSG00000185499. [P15941-9]
ENST00000368390; ENSP00000357375; ENSG00000185499. [P15941-7]
ENST00000368392; ENSP00000357377; ENSG00000185499. [P15941-11]
ENST00000368393; ENSP00000357378; ENSG00000185499. [P15941-13]
ENST00000368396; ENSP00000357381; ENSG00000185499. [P15941-12]
ENST00000368398; ENSP00000357383; ENSG00000185499. [P15941-6]
ENST00000457295; ENSP00000388172; ENSG00000185499. [P15941-17]
GeneID4582.
KEGGhsa:4582.
UCSCuc001fia.3. human. [P15941-7]
uc001fib.3. human. [P15941-10]
uc001fie.3. human. [P15941-9]
uc001fij.3. human.
uc001fik.3. human. [P15941-8]
uc001fin.3. human.
uc009wpm.3. human.

Organism-specific databases

CTD4582.
GeneCardsGC01M155158.
HGNCHGNC:7508. MUC1.
HPACAB000036.
CAB001986.
HPA004179.
HPA007235.
HPA008855.
MIM113720. gene.
158340. gene.
174000. phenotype.
neXtProtNX_P15941.
Orphanet34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
PharmGKBPA31309.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77744.
HOGENOMHOG000290201.
HOVERGENHBG003075.
KOK06568.
PhylomeDBP15941.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP15941.
BgeeP15941.
GenevestigatorP15941.

Family and domain databases

Gene3D3.30.70.960. 1 hit.
InterProIPR023217. Mucin-1.
IPR000082. SEA_dom.
[Graphical view]
PANTHERPTHR10006. PTHR10006. 1 hit.
PfamPF01390. SEA. 1 hit.
[Graphical view]
SMARTSM00200. SEA. 1 hit.
[Graphical view]
SUPFAMSSF82671. SSF82671. 1 hit.
PROSITEPS50024. SEA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMUC1. human.
EvolutionaryTraceP15941.
GeneWikiMUC1.
GenomeRNAi4582.
NextBio13635564.
PROP15941.
SOURCESearch...

Entry information

Entry nameMUC1_HUMAN
AccessionPrimary (citable) accession number: P15941
Secondary accession number(s): A5YRV1 expand/collapse secondary AC list , 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
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries