MUC1
entrez
4582
canonical
uniprot
P15941
canonical
ensembl
ENSG00000185499
resolver
ensp
ENSP00000338983
resolver
ensp
ENSP00000339690
resolver
ensp
ENSP00000343482
resolver
ensp
ENSP00000357374
resolver
ensp
ENSP00000357375
resolver
ensp
ENSP00000357377
resolver
ensp
ENSP00000357378
resolver
ensp
ENSP00000357381
resolver
ensp
ENSP00000357383
resolver
ensp
ENSP00000388172
resolver
ensp
ENSP00000389098
resolver
ensp
ENSP00000481231
resolver
ensp
ENSP00000483473
resolver
ensp
ENSP00000483482
resolver
ensp
ENSP00000484730
resolver
enst
ENST00000338684
resolver
enst
ENST00000610359
resolver
enst
ENST00000615517
resolver
enst
ENST00000620103
resolver
genesymbol
MUC1
resolver
genesymbol_syn
PUM
resolver
hgnc
HGNC:7508
resolver
uniprot
A0A087X0L0
resolver
uniprot
A0A087X0L2
resolver
uniprot
A0A0A0MRB3
resolver
uniprot
A0A0C4DGW3
resolver
uniprot
A0A384NPK6
resolver
uniprot
A5YRU5
resolver
uniprot
A5YRU7
resolver
uniprot
A5YRV0
resolver
uniprot
A5YRV1
resolver
uniprot
A5YRV2
resolver
uniprot
A6ZID6
resolver
uniprot
A6ZID7
resolver
uniprot
A6ZID9
resolver
uniprot
A6ZIE0
resolver
uniprot
A6ZIE4
resolver
uniprot
A6ZIE6
resolver
uniprot
B1AVQ8
resolver
uniprot
B1AVR0
resolver
uniprot
B6ECA1
resolver
uniprot
B6ECB3
resolver
uniprot
E7ESE5
resolver
uniprot
E7EUG9
resolver
uniprot
P13931
resolver
uniprot
P15942
resolver
uniprot
P17626
resolver
uniprot
Q0VAP5
resolver
uniprot
Q0VAP6
resolver
uniprot
Q14128
resolver
uniprot
Q14876
resolver
uniprot
Q16437
resolver
uniprot
Q16442
resolver
uniprot
Q16615
resolver
uniprot
Q6S4Y3
resolver
uniprot
Q7Z538
resolver
uniprot
Q7Z547
resolver
uniprot
Q7Z548
resolver
uniprot
Q7Z550
resolver
uniprot
Q7Z551
resolver
uniprot
Q7Z552
resolver
uniprot
Q9BXA4
resolver
uniprot
Q9UE75
resolver
uniprot
Q9UE76
resolver
uniprot
Q9UQL1
resolver
uniprot
Q9Y4J2
resolver
uniprot_entry
A0A087X0L0_HUMAN
resolver
uniprot_entry
A0A087X0L2_HUMAN
resolver
uniprot_entry
A0A0A0MRB3_HUMAN
resolver
uniprot_entry
A0A0C4DGW3_HUMAN
resolver
uniprot_entry
A0A384NPK6_HUMAN
resolver
uniprot_entry
A5YRU5_HUMAN
resolver
uniprot_entry
A5YRU7_HUMAN
resolver
uniprot_entry
A5YRV0_HUMAN
resolver
uniprot_entry
A5YRV2_HUMAN
resolver
uniprot_entry
A6ZID6_HUMAN
resolver
uniprot_entry
A6ZID7_HUMAN
resolver
uniprot_entry
A6ZIE4_HUMAN
resolver
uniprot_entry
A6ZIE6_HUMAN
resolver
uniprot_entry
B6ECB3_HUMAN
resolver
uniprot_entry
MUC1_HUMAN
resolver
uniprot_entry
Q7Z538_HUMAN
resolver
uniprot_entry
Q7Z551_HUMAN
resolver
uniprot_sec
A5YRV1
resolver
uniprot_sec
A6ZID9
resolver
uniprot_sec
A6ZIE0
resolver
uniprot_sec
B1AVQ8
resolver
uniprot_sec
B1AVR0
resolver
uniprot_sec
B6ECA1
resolver
uniprot_sec
E7ESE5
resolver
uniprot_sec
E7EUG9
resolver
uniprot_sec
P13931
resolver
uniprot_sec
P15942
resolver
uniprot_sec
P17626
resolver
uniprot_sec
Q0VAP5
resolver
uniprot_sec
Q0VAP6
resolver
uniprot_sec
Q14128
resolver
uniprot_sec
Q14876
resolver
uniprot_sec
Q16437
resolver
uniprot_sec
Q16442
resolver
uniprot_sec
Q16615
resolver
uniprot_sec
Q6S4Y3
resolver
uniprot_sec
Q7Z547
resolver
uniprot_sec
Q7Z548
resolver
uniprot_sec
Q7Z550
resolver
uniprot_sec
Q7Z552
resolver
uniprot_sec
Q9BXA4
resolver
uniprot_sec
Q9UE75
resolver
uniprot_sec
Q9UE76
resolver
uniprot_sec
Q9UQL1
resolver
uniprot_sec
Q9Y4J2
resolver
amino_acid_sequence
MTPGTQSPFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTSAPDNKPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDNRPALGSTAPPVHNVTSASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLASHSTKTDASSTHHSSVPPLTSSNHSTSPQLSTGVSFFFLSFHISNLQFNSSLEDPSTDYYQELQRDISEMFLQIYKQGGFLGLSNIKFRPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL
uniprot
proteins
disease_involvement
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: Tubulointerstitial kidney disease, autosomal dominant 2 (ADTKD2) [MIM:174000]: A form of autosomal dominant tubulointerstitial kidney disease, a genetically heterogeneous disorder characterized by slowly progressive loss of kidney function, bland urinary sediment, hyperuricemia, absent or mildly increased albuminuria, lack of severe hypertension during the early stages, and normal or small kidneys on ultrasound. Renal histology shows variable abnormalities including interstitial fibrosis with tubular atrophy, microcystic dilatation of the tubules, thickening of tubular basement membranes, medullary cysts, and secondary glomerulosclerotic or glomerulocystic changes with abnormal glomerular tufting. There is significant variability, as well as incomplete penetrance. {ECO:0000269|PubMed:23396133}. Note=The disease is caused by variants affecting the gene represented in this entry.
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-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.
uniprot
proteins
mass_dalton
122102
uniprot
proteins
mutagenesis
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
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
pubmed
10197628
uniprot
proteins
pubmed
10373415
uniprot
proteins
pubmed
11118479
uniprot
proteins
pubmed
11152665
uniprot
proteins
pubmed
11173916
uniprot
proteins
pubmed
11341784
uniprot
proteins
pubmed
11350974
uniprot
proteins
pubmed
11483589
uniprot
proteins
pubmed
11877440
uniprot
proteins
pubmed
12441351
uniprot
proteins
pubmed
12750561
uniprot
proteins
pubmed
12832415
uniprot
proteins
pubmed
12939402
uniprot
proteins
pubmed
14521915
uniprot
proteins
pubmed
14688481
uniprot
proteins
pubmed
15471854
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15513966
uniprot
proteins
pubmed
15623537
uniprot
proteins
pubmed
15710329
uniprot
proteins
pubmed
15969018
uniprot
proteins
pubmed
15972891
uniprot
proteins
pubmed
15987679
uniprot
proteins
pubmed
16288032
uniprot
proteins
pubmed
16427018
uniprot
proteins
pubmed
16507569
uniprot
proteins
pubmed
16585136
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
1688329
uniprot
proteins
pubmed
1697589
uniprot
proteins
pubmed
16983337
uniprot
proteins
pubmed
17308127
uniprot
proteins
pubmed
17524503
uniprot
proteins
pubmed
17545600
uniprot
proteins
pubmed
20816948
uniprot
proteins
pubmed
2112460
uniprot
proteins
pubmed
2268309
uniprot
proteins
pubmed
22941036
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
2318825
uniprot
proteins
pubmed
23396133
uniprot
proteins
pubmed
2351132
uniprot
proteins
pubmed
2394722
uniprot
proteins
pubmed
2597151
uniprot
proteins
pubmed
3417635
uniprot
proteins
pubmed
35504880
uniprot
proteins
pubmed
7664271
uniprot
proteins
pubmed
7744025
uniprot
proteins
pubmed
7925397
uniprot
proteins
pubmed
7988707
uniprot
proteins
pubmed
8604237
uniprot
proteins
pubmed
8608966
uniprot
proteins
pubmed
9139698
uniprot
proteins
pubmed
9212228
uniprot
proteins
pubmed
9312074
uniprot
proteins
pubmed
9536947
uniprot
proteins
pubmed
9597769
uniprot
proteins
pubmed
9819408
uniprot
proteins
sequence_length
1255
uniprot
proteins
subcellular_location
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.
uniprot
proteins
transmembrane_region
TRANSMEM 1159..1181; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins