Mucin 1 Antibody (YA3817)

Apical cell membrane; Single-pass type I membrane protein; Secreted; Secreted; Secreted; Cell membrane; Cytoplasm; Nucleus

Tissue_specificity:It is expressed on the apical surface of epithelial cells, particularly in respiratory, breast, and uterine epithelial cells. It is also expressed in both activated and inactivated T cells. It is overexpressed in epithelial tumors such as breast or ovarian cancer, as well as in non-epithelial tumor cells. The Y isotype is expressed only in tumor cells.

P15941 has 17 isomers: P15941-1: 122102 Da (predicted); P15941-2: 122941 Da (predicted); P15941-3: 121803 Da (predicted); P15941-4: 121021 Da (predicted); P15941-5: 103836 Da (predicted); P15941-6: 24566 Da (predicted); P15941-7: 27566 Da (predicted); P15941-8: 29592 Da (predicted); P15941-9: 18277 Da (predicted); P15941-10: 21556 Da (predicted); P15941-11: 28405 Da (predicted); P15941-12: 17090 Da (predicted); P15941-13: 21663 Da (predicted); P15941-14: 10403 Da (predicted); P15941-15: 23747 Da (predicted); P15941-16: 17287 Da (predicted); P15941-17: 28297 Da (predicted).
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;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;Dual palmitoylation on cysteine residues in the CQC motif is required for recycling from endosomes back to the plasma membrane;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;The N-terminal sequence has been shown to begin at position 24 or 28

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

P15941

MUC1; EMA; MCD; PEM; PUM; KL-6; MAM6; MCKD; PEMT; H23AG; MCKD1; MUC-1; ADMCKD; ADMCKD1; CA 15-3; MUC-1/X; MUC1/ZD; MUC-1/SEC