Muc1
entrez
17829
canonical
uniprot
Q02496
canonical
ensembl
ENSMUSG00000042784
resolver
ensp
ENSMUSP00000041963
resolver
enst
ENSMUST00000041142
resolver
genesymbol
Muc1
resolver
genesymbol_syn
Muc-1
resolver
uniprot
A0A0R4J0H1
resolver
uniprot_entry
A0A0R4J0H1_MOUSE
resolver
uniprot_entry
MUC1_MOUSE
resolver
amino_acid_sequence
MTPGIRAPFFLLLLLASLKGFLALPSEENSVTSSQDTSSSLASTTTPVHSSNSDPATRPPGDSTSSPVQSSTSSPATRAPEDSTSTAVLSGTSSPATTAPVNSASSPVAHGDTSSPATSLSKDSNSSPVVHSGTSSAATTAPVDSTSSPVVHGGTSSPATSPPGDSTSSPDHSSTSSPATRAPEDSTSTAVLSGTSSPATTAPVDSTSSPVAHDDTSSPATSLSEDSASSPVAHGGTSSPATSPLRDSTSSPVHSSASIQNIKTTSDLASTPDHNGTSVTTTSSALGSATSPDHSGTSTTTNSSESVLATTPVYSSMPFSTTKVTSGSAIIPDHNGSSVLPTSSVLGSATSLVYNTSAIATTPVSNGTQPSVPSQYPVSPTMATTSSHSTIASSSYYSTVPFSTFSSNSSPQLSVGVSFFFLSFYIQNHPFNSSLEDPSSNYYQELKRNISGLFLQIFNGDFLGISSIKFRSGSVVVESTVVFREGTFSASDVKSQLIQHKKEADDYNLTISEVKVNEMQFPPSAQSRPGVPGWGIALLVLVCILVALAIVYFLALAVCQCRRKSYGQLDIFPTQDTYHPMSEYPTYHTHGRYVPPGSTKRSPYEEVSAGNGSSSLSYTNPAVVTTSANL
uniprot
proteins
function
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-kappaB pathways. In activated T-cells, influences directly or indirectly the Ras/MAPK pathway. Regulates P53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of P53 and represses P53 activity.
uniprot
proteins
mass_dalton
64539
uniprot
proteins
post_translational_modification
PTM: Probably both N- and extensively O-glycosylated (in repeat region).; 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. Ectodomain shedding is mediated by ADAM17 in uterine epithelial cells (By similarity). {ECO:0000250}.; PTM: Dual palmitoylation on cysteine residues in the CQC motif is required for recycling from endosomes back to the plasma membrane. {ECO:0000250}.; 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. Csk- or Src- or EGFR-mediated phosphorylation on Tyr-604 increases binding to beta-catenin/CTNNB1. GSK3B-mediated phosphorylation on Ser-602 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 (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
1714452
uniprot
proteins
pubmed
17641781
uniprot
proteins
pubmed
1958179
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
630
uniprot
proteins
subcellular_location
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 (By similarity). {ECO:0000250}.; 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 (By similarity). Some transportation to the nucleus when infected with C.jejeuni. {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 536..556; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins