Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P15941

- MUC1_HUMAN

UniProt

P15941 - MUC1_HUMAN

Protein

Mucin-1

Gene

MUC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.
    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1097 – 10982Cleavage; by autolysis

    GO - Molecular functioni

    1. p53 binding Source: BHF-UCL
    2. protein binding Source: IntAct
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
    4. transcription cofactor activity Source: BHF-UCL

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: BHF-UCL
    3. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: BHF-UCL
    4. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
    5. negative regulation of transcription by competitive promoter binding Source: BHF-UCL
    6. O-glycan processing Source: Reactome
    7. positive regulation of histone H4 acetylation Source: BHF-UCL
    8. positive regulation of transcription from RNA polymerase II promoter in response to stress Source: BHF-UCL
    9. post-translational protein modification Source: Reactome
    10. regulation of transcription from RNA polymerase II promoter in response to stress Source: BHF-UCL

    Enzyme and pathway databases

    ReactomeiREACT_115606. O-linked glycosylation of mucins.
    REACT_115835. Termination of O-glycan biosynthesis.

    Protein family/group databases

    MEROPSiS71.001.

    Names & Taxonomyi

    Protein namesi
    Recommended 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:
    Mucin-1 subunit alpha
    Short name:
    MUC1-NT
    Short name:
    MUC1-alpha
    Mucin-1 subunit beta
    Short name:
    MUC1-beta
    Alternative name(s):
    MUC1-CT
    Gene namesi
    Name:MUC1
    Synonyms:PUM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7508. MUC1.

    Subcellular locationi

    Apical cell membrane 8 Publications; Single-pass type I membrane protein 8 Publications
    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.
    Chain 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.

    GO - Cellular componenti

    1. apical plasma membrane Source: RefGenome
    2. cell surface Source: RefGenome
    3. cytoplasm Source: RefGenome
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi lumen Source: Reactome
    7. integral component of plasma membrane Source: ProtInc
    8. nuclear chromatin Source: BHF-UCL
    9. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus, Secreted

    Pathology & Biotechi

    Involvement in diseasei

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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1098 – 10981S → A, D, E, F, G, H, I, K, L, M, N, P, Q, R, V, W or Y: Completely abrogates cleavage. 2 Publications
    Mutagenesisi1098 – 10981S → C or T: Almost complete cleavage. 2 Publications
    Mutagenesisi1116 – 11161D → A: Greatly reduced formation of isoform 5/isoform Y complex. 2 Publications
    Mutagenesisi1116 – 11161D → E: No effect on formation of isoform 5/isoform Y complex. 2 Publications
    Mutagenesisi1184 – 11841C → 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. 2 Publications
    Mutagenesisi1186 – 11861C → 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. 2 Publications
    Mutagenesisi1187 – 11893RRK → AAA: No nuclear targeting of HRG-stimulated MUC1 C-terminal nor JUP/gamma-catenin. No effect on interaction with JUP/gamma-catenin. 1 Publication
    Mutagenesisi1187 – 11893RRK → QQQ: No effect on palmitoylation. 1 Publication
    Mutagenesisi1191 – 11911Y → F: No effect on EGFR-mediated phosphorylation. 3 Publications
    Mutagenesisi1191 – 11911Y → N: No effect on endocytosis. 3 Publications
    Mutagenesisi1203 – 12031Y → E: No effect on nuclear colocalization of MUC1CT and CTNNB1. No effect on in vitro PDFGR-induced cell invasiveness. 5 Publications
    Mutagenesisi1203 – 12031Y → F: No effect on EGFR-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-induced cell invasiveness. 5 Publications
    Mutagenesisi1203 – 12031Y → 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. 5 Publications
    Mutagenesisi1209 – 12091Y → F: Some reduction in EGFR-mediated phosphorylation. 2 Publications
    Mutagenesisi1218 – 12181Y → F: No effect on EGFR-mediated phosphorylation. No nuclear colocalization of MUC1CT and CTNNB1. 3 Publications
    Mutagenesisi1223 – 12231S → A: No change in PRKCD- nor GSK3B-mediated phosphorylation. 3 Publications
    Mutagenesisi1224 – 12241T → 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. 2 Publications
    Mutagenesisi1227 – 12271S → A: No change in PRKCD-mediated phosphorylation. Loss of GSK3B-mediated phosphorylation. CTNNB1. 3 Publications
    Mutagenesisi1229 – 12291Y → F: Greatly reduced EGFR- and Src-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-mediated phosphorylation. Decreased Src-binding. 5 Publications
    Mutagenesisi1229 – 12291Y → N: No effect on endocytosis. 5 Publications
    Mutagenesisi1243 – 12431Y → 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. 2 Publications

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    MIMi174000. phenotype.
    Orphaneti34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
    PharmGKBiPA31309.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23232 PublicationsAdd
    BLAST
    Chaini24 – 12551232Mucin-1PRO_0000019277Add
    BLAST
    Chaini24 – 10971074Mucin-1 subunit alphaPRO_0000317446Add
    BLAST
    Chaini1098 – 1255158Mucin-1 subunit betaPRO_0000317447Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi131 – 1311O-linked (GalNAc...)2 Publications
    Glycosylationi139 – 1391O-linked (GalNAc...)2 Publications
    Glycosylationi140 – 1401O-linked (GalNAc...)Sequence Analysis
    Glycosylationi144 – 1441O-linked (GalNAc...)Sequence Analysis
    Glycosylationi957 – 9571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi975 – 9751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1029 – 10291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1055 – 10551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1133 – 11331N-linked (GlcNAc...)Sequence Analysis
    Lipidationi1184 – 11841S-palmitoyl cysteine1 Publication
    Lipidationi1186 – 11861S-palmitoyl cysteine1 Publication
    Modified residuei1191 – 11911Phosphotyrosine
    Modified residuei1203 – 12031Phosphotyrosine; by PDGFR2 Publications
    Modified residuei1209 – 12091Phosphotyrosine
    Modified residuei1212 – 12121Phosphotyrosine1 Publication
    Modified residuei1218 – 12181Phosphotyrosine; by PDGFR1 Publication
    Modified residuei1224 – 12241Phosphothreonine; by PKC/PRKCD1 Publication
    Modified residuei1227 – 12271Phosphoserine; by GSK3-beta1 Publication
    Modified residuei1229 – 12291Phosphotyrosine; by CSK, EGFR and SRC4 Publications
    Modified residuei1243 – 12431Phosphotyrosine1 Publication

    Post-translational modificationi

    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.4 Publications
    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 ADAM17.3 Publications
    Dual palmitoylation on cysteine residues in the CQC motif is required for recycling from endosomes back to the plasma membrane.1 Publication
    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 CTNNB1.11 Publications
    The N-terminal sequence has been shown to begin at position 24 or 28.1 Publication

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP15941.
    PaxDbiP15941.
    PRIDEiP15941.

    PTM databases

    PhosphoSiteiP15941.
    UniCarbKBiP15941.

    Expressioni

    Tissue specificityi

    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 7 is expressed in tumor cells only.2 Publications

    Developmental stagei

    During fetal development, expressed at low levels in the colonic epithelium from 13 weeks of gestation.1 Publication

    Gene expression databases

    ArrayExpressiP15941.
    BgeeiP15941.
    GenevestigatoriP15941.

    Organism-specific databases

    HPAiCAB000036.
    CAB001986.
    HPA004179.
    HPA007235.
    HPA008855.

    Interactioni

    Subunit structurei

    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.21 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005198EBI-2804728,EBI-375543
    METP085812EBI-2804728,EBI-1039152
    MUC1P15941-72EBI-2804728,EBI-4396776
    U2AF2P263682EBI-2804728,EBI-742339

    Protein-protein interaction databases

    BioGridi110669. 29 interactions.
    DIPiDIP-41890N.
    IntActiP15941. 8 interactions.
    MINTiMINT-156679.

    Structurei

    Secondary structure

    1
    1255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1042 – 105211
    Helixi1056 – 10594
    Helixi1064 – 108017
    Turni1082 – 10854
    Beta strandi1086 – 109611
    Beta strandi1099 – 11079
    Turni1109 – 11113
    Helixi1114 – 113219
    Beta strandi1136 – 11427

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SM3X-ray1.95P919-931[»]
    2ACMNMR-A1042-1097[»]
    B1098-1152[»]
    2FO4X-ray2.70P140-146[»]
    ProteinModelPortaliP15941.
    SMRiP15941. Positions 1041-1144.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15941.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 11581135ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1182 – 125574CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1159 – 118123HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati61 – 80201; approximate1 PublicationAdd
    BLAST
    Repeati81 – 100202; approximate1 PublicationAdd
    BLAST
    Repeati101 – 1202031 PublicationAdd
    BLAST
    Repeati121 – 1402041 PublicationAdd
    BLAST
    Repeati141 – 1602051 PublicationAdd
    BLAST
    Repeati161 – 1802061 PublicationAdd
    BLAST
    Repeati181 – 2002071 PublicationAdd
    BLAST
    Repeati201 – 2202081 PublicationAdd
    BLAST
    Repeati221 – 2402091 PublicationAdd
    BLAST
    Repeati241 – 26020101 PublicationAdd
    BLAST
    Repeati261 – 28020111 PublicationAdd
    BLAST
    Repeati281 – 30020121 PublicationAdd
    BLAST
    Repeati301 – 32020131 PublicationAdd
    BLAST
    Repeati321 – 34020141 PublicationAdd
    BLAST
    Repeati341 – 36020151 PublicationAdd
    BLAST
    Repeati361 – 38020161 PublicationAdd
    BLAST
    Repeati381 – 40020171 PublicationAdd
    BLAST
    Repeati401 – 42020181 PublicationAdd
    BLAST
    Repeati421 – 44020191 PublicationAdd
    BLAST
    Repeati441 – 46020201 PublicationAdd
    BLAST
    Repeati461 – 48020211 PublicationAdd
    BLAST
    Repeati481 – 50020221 PublicationAdd
    BLAST
    Repeati501 – 52020231 PublicationAdd
    BLAST
    Repeati521 – 54020241 PublicationAdd
    BLAST
    Repeati541 – 56020251 PublicationAdd
    BLAST
    Repeati561 – 58020261 PublicationAdd
    BLAST
    Repeati581 – 60020271 PublicationAdd
    BLAST
    Repeati601 – 62020281 PublicationAdd
    BLAST
    Repeati621 – 64020291 PublicationAdd
    BLAST
    Repeati641 – 66020301 PublicationAdd
    BLAST
    Repeati661 – 68020311 PublicationAdd
    BLAST
    Repeati681 – 70020321 PublicationAdd
    BLAST
    Repeati701 – 72020331 PublicationAdd
    BLAST
    Repeati721 – 74020341 PublicationAdd
    BLAST
    Repeati741 – 76020351 PublicationAdd
    BLAST
    Repeati761 – 78020361 PublicationAdd
    BLAST
    Repeati781 – 80020371 PublicationAdd
    BLAST
    Repeati801 – 82020381 PublicationAdd
    BLAST
    Repeati821 – 84020391 PublicationAdd
    BLAST
    Repeati841 – 86020401 PublicationAdd
    BLAST
    Repeati861 – 88020411 PublicationAdd
    BLAST
    Repeati881 – 90020421 PublicationAdd
    BLAST
    Repeati901 – 92020431 PublicationAdd
    BLAST
    Repeati921 – 94020441 PublicationAdd
    BLAST
    Repeati941 – 96020451 PublicationAdd
    BLAST
    Repeati961 – 9802046; approximate1 PublicationAdd
    BLAST
    Repeati981 – 10002047; approximate1 PublicationAdd
    BLAST
    Repeati1001 – 10202048; approximate1 PublicationAdd
    BLAST
    Domaini1039 – 1148110SEAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni126 – 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-RAdd
    BLAST
    Regioni1192 – 122837Interaction with P53Add
    BLAST
    Regioni1223 – 12308Required for interaction with GSK3B
    Regioni1233 – 12419Required for interaction with beta- and gamma-catenins

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1203 – 12064Interaction with GRB2
    Motifi1229 – 12324Interaction with SRC and ESR1
    Motifi1243 – 12464Required for interaction with AP1S2

    Sequence similaritiesi

    Contains 1 SEA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG77744.
    HOGENOMiHOG000290201.
    HOVERGENiHBG003075.
    KOiK06568.
    PhylomeDBiP15941.

    Family and domain databases

    Gene3Di3.30.70.960. 1 hit.
    InterProiIPR023217. Mucin-1.
    IPR000082. SEA_dom.
    [Graphical view]
    PANTHERiPTHR10006:SF5. PTHR10006:SF5. 1 hit.
    PfamiPF01390. SEA. 1 hit.
    [Graphical view]
    SMARTiSM00200. SEA. 1 hit.
    [Graphical view]
    SUPFAMiSSF82671. SSF82671. 1 hit.
    PROSITEiPS50024. SEA. 1 hit.
    [Graphical view]

    Sequences (17)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 17 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P15941-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE     50
    KNAVSMTSSV LSSHSPGSGS STTQGQDVTL APATEPASGS AATWGQDVTS 100
    VPVTRPALGS TTPPAHDVTS APDNKPAPGS TAPPAHGVTS APDTRPAPGS 150
    TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 200
    APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS 250
    TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 300
    APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS 350
    TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 400
    APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS 450
    TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 500
    APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS 550
    TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 600
    APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS 650
    TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 700
    APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS 750
    TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 800
    APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS 850
    TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 900
    APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDNRPALGS 950
    TAPPVHNVTS ASGSASGSAS TLVHNGTSAR ATTTPASKST PFSIPSHHSD 1000
    TPTTLASHST KTDASSTHHS SVPPLTSSNH STSPQLSTGV SFFFLSFHIS 1050
    NLQFNSSLED PSTDYYQELQ RDISEMFLQI YKQGGFLGLS NIKFRPGSVV 1100
    VQLTLAFREG TINVHDVETQ FNQYKTEAAS RYNLTISDVS VSDVPFPFSA 1150
    QSGAGVPGWG IALLVLVCVL VALAIVYLIA LAVCQCRRKN YGQLDIFPAR 1200
    DTYHPMSEYP TYHTHGRYVP PSSTDRSPYE KVSAGNGGSS LSYTNPAVAA 1250
    TSANL 1255
    Length:1,255
    Mass (Da):122,102
    Last modified:May 18, 2010 - v3
    Checksum:i5E28DFC4C20D9A82
    GO
    Isoform 2 (identifier: P15941-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         19-19: T → TATTAPKPAT

    Show »
    Length:1,264
    Mass (Da):122,941
    Checksum:i3810149471D221FD
    GO
    Isoform 3 (identifier: P15941-3) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         19-21: Missing.

    Show »
    Length:1,252
    Mass (Da):121,803
    Checksum:iA3F30DBFE56DD0C5
    GO
    Isoform 4 (identifier: P15941-4) [UniParc]FASTAAdd to Basket

    Also known as: D

    The sequence of this isoform differs from the canonical sequence as follows:
         20-31: Missing.

    Show »
    Length:1,243
    Mass (Da):121,021
    Checksum:iB2C6288C94AABC14
    GO
    Isoform 5 (identifier: P15941-5) [UniParc]FASTAAdd to Basket

    Also known as: SEC

    The sequence of this isoform differs from the canonical sequence as follows:
         1077-1087: FLQIYKQGGFL → VSIGLSFPMLP
         1088-1255: Missing.

    Show »
    Length:1,087
    Mass (Da):103,836
    Checksum:i6039CBB69974EA3E
    GO
    Isoform 6 (identifier: P15941-6) [UniParc]FASTAAdd to Basket

    Also known as: X

    The sequence of this isoform differs from the canonical sequence as follows:
         54-70: VSMTSSVLSSHSPGSGS → IPAPTTTKSCRETFLKW
         71-1095: Missing.

    Show »
    Length:230
    Mass (Da):24,566
    Checksum:i53B036250EC1242D
    GO
    Isoform Y (identifier: P15941-7) [UniParc]FASTAAdd to Basket

    Also known as: MUC1/Y

    The sequence of this isoform differs from the canonical sequence as follows:
         54-1053: Missing.

    Show »
    Length:255
    Mass (Da):27,566
    Checksum:i46DC2580CF357BEF
    GO
    Isoform 8 (identifier: P15941-8) [UniParc]FASTAAdd to Basket

    Also known as: Z

    The sequence of this isoform differs from the canonical sequence as follows:
         54-1035: Missing.

    Show »
    Length:273
    Mass (Da):29,592
    Checksum:iB72F7F4FC2D23BCC
    GO
    Isoform 9 (identifier: P15941-9) [UniParc]FASTAAdd to Basket

    Also known as: S

    The sequence of this isoform differs from the canonical sequence as follows:
         54-1035: Missing.
         1077-1181: Missing.

    Show »
    Length:168
    Mass (Da):18,277
    Checksum:i53C6544C2B077B89
    GO
    Isoform F (identifier: P15941-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         54-87: VSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPA → IPAPTTTKSCRETFLKCFCRFINKGVFWASPILS
         88-1139: Missing.

    Show »
    Length:203
    Mass (Da):21,556
    Checksum:iCC2BE70F8C1B325E
    GO
    Isoform Y-LSP (identifier: P15941-11) [UniParc]FASTAAdd to Basket

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

    Note: Lacks the mucin repeats.

    Show »
    Length:264
    Mass (Da):28,405
    Checksum:i6E192550756A6D4A
    GO
    Isoform S2 (identifier: P15941-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         19-19: T → TATTAPKPAT
         54-1053: Missing.
         1077-1181: Missing.

    Show »
    Length:159
    Mass (Da):17,090
    Checksum:i2C3B69F515D73168
    GO
    Isoform M6 (identifier: P15941-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         54-1035: Missing.
         1141-1180: VSDVPFPFSA...VALAIVYLIA → GCLSVPPKEL...LPHPWALCAP
         1181-1255: Missing.

    Show »
    Length:198
    Mass (Da):21,663
    Checksum:i5300166458B017CB
    GO
    Isoform ZD (identifier: P15941-14) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:96
    Mass (Da):10,403
    Checksum:iF2140812C4C11983
    GO
    Isoform T10 (identifier: P15941-15) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         19-19: T → TATTAPKPAT
         54-1093: Missing.

    Show »
    Length:224
    Mass (Da):23,747
    Checksum:i977E7703C14AC936
    GO
    Isoform E2 (identifier: P15941-16) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         19-19: T → TATTAPKPAT
         54-1151: Missing.

    Show »
    Length:166
    Mass (Da):17,287
    Checksum:iBF6C969984986AD0
    GO
    Isoform J13 (identifier: P15941-17) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:259
    Mass (Da):28,297
    Checksum:iFD53C9223E24B094
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21T → A in AAD14369. (PubMed:8604237)Curated
    Sequence conflicti134 – 1341P → Q in AAA35757. (PubMed:2597151)Curated
    Sequence conflicti154 – 1541P → Q in AAA35757. (PubMed:2597151)Curated
    Sequence conflicti1021 – 10211S → T in AAA35805. (PubMed:2318825)Curated
    Sequence conflicti1021 – 10211S → T in AAA35807. (PubMed:2318825)Curated
    Sequence conflicti1021 – 10211S → T in AAA59876. (PubMed:1697589)Curated
    Sequence conflicti1143 – 11431D → G in AAP97018. (PubMed:22941036)Curated
    Sequence conflicti1193 – 11931Q → L in AAK30142. (PubMed:15969018)Curated
    Sequence conflicti1231 – 12311K → T in AAD10858. (PubMed:9212228)Curated
    Sequence conflicti1251 – 12511T → A in AAA60019. (PubMed:2394722)Curated

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1117 – 11171V → M.3 Publications
    Corresponds to variant rs1611770 [ dbSNP | Ensembl ].
    VAR_019390
    Natural varianti1142 – 11421S → N.1 Publication
    Corresponds to variant rs11465207 [ dbSNP | Ensembl ].
    VAR_019391

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei19 – 213Missing in isoform 3. 1 PublicationVSP_003281
    Alternative sequencei19 – 191T → TATTAPKPAT in isoform 2, isoform Y-LSP, isoform E2, isoform J13, isoform S2 and isoform T10. 6 PublicationsVSP_003280
    Alternative sequencei20 – 3112Missing in isoform 4. 1 PublicationVSP_003282Add
    BLAST
    Alternative sequencei54 – 11511098Missing in isoform E2. 1 PublicationVSP_047872Add
    BLAST
    Alternative sequencei54 – 10931040Missing in isoform T10. 1 PublicationVSP_047873Add
    BLAST
    Alternative sequencei54 – 10531000Missing in isoform J13, isoform Y, isoform Y-LSP and isoform S2. 6 PublicationsVSP_003285Add
    BLAST
    Alternative sequencei54 – 1035982Missing in isoform 8, isoform 9 and isoform M6. 4 PublicationsVSP_003286Add
    BLAST
    Alternative sequencei54 – 9643VSMTS…ATWGQ → IPAPTTTKSCRETFLKCFCR FINKGVFWASPILSSGQDLW WYN in isoform ZD. 2 PublicationsVSP_047575Add
    BLAST
    Alternative sequencei54 – 8734VSMTS…ATEPA → IPAPTTTKSCRETFLKCFCR FINKGVFWASPILS in isoform F. 1 PublicationVSP_035046Add
    BLAST
    Alternative sequencei54 – 7017VSMTS…PGSGS → IPAPTTTKSCRETFLKW in isoform 6. 2 PublicationsVSP_003283Add
    BLAST
    Alternative sequencei71 – 10951025Missing in isoform 6. 2 PublicationsVSP_003284Add
    BLAST
    Alternative sequencei88 – 11391052Missing in isoform F. 1 PublicationVSP_035047Add
    BLAST
    Alternative sequencei97 – 12551159Missing in isoform ZD. 2 PublicationsVSP_047576Add
    BLAST
    Alternative sequencei1077 – 1181105Missing in isoform 9 and isoform S2. 3 PublicationsVSP_003287Add
    BLAST
    Alternative sequencei1077 – 108711FLQIYKQGGFL → VSIGLSFPMLP in isoform 5. 1 PublicationVSP_003288Add
    BLAST
    Alternative sequencei1088 – 1255168Missing in isoform 5. 1 PublicationVSP_003289Add
    BLAST
    Alternative sequencei1141 – 118040VSDVP…VYLIA → GCLSVPPKELRAAGHLSSPG YLPSYERVPHLPHPWALCAP in isoform M6. 2 PublicationsVSP_046962Add
    BLAST
    Alternative sequencei1181 – 125575Missing in isoform M6. 2 PublicationsVSP_046963Add
    BLAST
    Alternative sequencei1232 – 125524VSAGN…TSANL → RQNGWSTMPRGALPEESQG in isoform J13. 1 PublicationVSP_047874Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1098.1. [P15941-8]
    CCDS30882.1. [P15941-11]
    CCDS30883.1. [P15941-7]
    CCDS41408.1. [P15941-12]
    CCDS41409.1. [P15941-10]
    CCDS55641.1. [P15941-6]
    CCDS55642.1. [P15941-13]
    PIRiA35175.
    RefSeqiNP_001018016.1. NM_001018016.2. [P15941-11]
    NP_001018017.1. NM_001018017.2. [P15941-7]
    NP_001037855.1. NM_001044390.2. [P15941-10]
    NP_001037856.1. NM_001044391.2.
    NP_001037857.1. NM_001044392.2. [P15941-12]
    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. [P15941-13]
    NP_001191223.1. NM_001204294.1. [P15941-6]
    NP_001191224.1. NM_001204295.1.
    NP_001191225.1. NM_001204296.1.
    NP_001191226.1. NM_001204297.1.
    NP_002447.4. NM_002456.5. [P15941-8]
    UniGeneiHs.89603.

    Genome annotation databases

    EnsembliENST00000337604; 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]
    GeneIDi4582.
    KEGGihsa:4582.
    UCSCiuc001fia.3. human. [P15941-7]
    uc001fib.3. human. [P15941-10]
    uc001fid.3. human.
    uc001fie.3. human. [P15941-9]
    uc001fij.3. human.
    uc001fik.3. human. [P15941-8]
    uc001fin.3. human.
    uc009wpm.3. human.

    Polymorphism databases

    DMDMi296439295.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Mucin database
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS1098.1. [P15941-8 ]
    CCDS30882.1. [P15941-11 ]
    CCDS30883.1. [P15941-7 ]
    CCDS41408.1. [P15941-12 ]
    CCDS41409.1. [P15941-10 ]
    CCDS55641.1. [P15941-6 ]
    CCDS55642.1. [P15941-13 ]
    PIRi A35175.
    RefSeqi NP_001018016.1. NM_001018016.2. [P15941-11 ]
    NP_001018017.1. NM_001018017.2. [P15941-7 ]
    NP_001037855.1. NM_001044390.2. [P15941-10 ]
    NP_001037856.1. NM_001044391.2.
    NP_001037857.1. NM_001044392.2. [P15941-12 ]
    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. [P15941-13 ]
    NP_001191223.1. NM_001204294.1. [P15941-6 ]
    NP_001191224.1. NM_001204295.1.
    NP_001191225.1. NM_001204296.1.
    NP_001191226.1. NM_001204297.1.
    NP_002447.4. NM_002456.5. [P15941-8 ]
    UniGenei Hs.89603.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SM3 X-ray 1.95 P 919-931 [» ]
    2ACM NMR - A 1042-1097 [» ]
    B 1098-1152 [» ]
    2FO4 X-ray 2.70 P 140-146 [» ]
    ProteinModelPortali P15941.
    SMRi P15941. Positions 1041-1144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110669. 29 interactions.
    DIPi DIP-41890N.
    IntActi P15941. 8 interactions.
    MINTi MINT-156679.

    Protein family/group databases

    MEROPSi S71.001.

    PTM databases

    PhosphoSitei P15941.
    UniCarbKBi P15941.

    Polymorphism databases

    DMDMi 296439295.

    Proteomic databases

    MaxQBi P15941.
    PaxDbi P15941.
    PRIDEi P15941.

    Protocols and materials databases

    DNASUi 4582.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337604 ; 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 ]
    GeneIDi 4582.
    KEGGi hsa:4582.
    UCSCi uc001fia.3. human. [P15941-7 ]
    uc001fib.3. human. [P15941-10 ]
    uc001fid.3. human.
    uc001fie.3. human. [P15941-9 ]
    uc001fij.3. human.
    uc001fik.3. human. [P15941-8 ]
    uc001fin.3. human.
    uc009wpm.3. human.

    Organism-specific databases

    CTDi 4582.
    GeneCardsi GC01M155158.
    GeneReviewsi MUC1.
    HGNCi HGNC:7508. MUC1.
    HPAi CAB000036.
    CAB001986.
    HPA004179.
    HPA007235.
    HPA008855.
    MIMi 113720. gene.
    158340. gene.
    174000. phenotype.
    neXtProti NX_P15941.
    Orphaneti 34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
    PharmGKBi PA31309.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG77744.
    HOGENOMi HOG000290201.
    HOVERGENi HBG003075.
    KOi K06568.
    PhylomeDBi P15941.

    Enzyme and pathway databases

    Reactomei REACT_115606. O-linked glycosylation of mucins.
    REACT_115835. Termination of O-glycan biosynthesis.

    Miscellaneous databases

    ChiTaRSi MUC1. human.
    EvolutionaryTracei P15941.
    GeneWikii MUC1.
    GenomeRNAii 4582.
    NextBioi 13635564.
    PROi P15941.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15941.
    Bgeei P15941.
    Genevestigatori P15941.

    Family and domain databases

    Gene3Di 3.30.70.960. 1 hit.
    InterProi IPR023217. Mucin-1.
    IPR000082. SEA_dom.
    [Graphical view ]
    PANTHERi PTHR10006:SF5. PTHR10006:SF5. 1 hit.
    Pfami PF01390. SEA. 1 hit.
    [Graphical view ]
    SMARTi SM00200. SEA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82671. SSF82671. 1 hit.
    PROSITEi PS50024. SEA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. Cited for: PROTEIN SEQUENCE OF 24-33; 28-37 AND 1098-1107, PROTEOLYTIC PROCESSING.
    27. 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. 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. 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. 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.

    Entry informationi

    Entry nameiMUC1_HUMAN
    AccessioniPrimary (citable) accession number: P15941
    Secondary accession number(s): 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
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 166 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3