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Q02496

- MUC1_MOUSE

UniProt

Q02496 - MUC1_MOUSE

Protein

Mucin-1

Gene

Muc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      Previous versions | rss
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    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-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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei473 – 4742Cleavage; by autolysisBy similarity

    GO - Biological processi

    1. cellular response to retinoic acid Source: Ensembl
    2. epithelial cell differentiation Source: Ensembl
    3. female pregnancy Source: Ensembl
    4. response to hypoxia Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_198517. O-linked glycosylation of mucins.
    REACT_198575. 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):
    Episialin
    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:Muc-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:97231. Muc1.

    Subcellular locationi

    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.By similarity
    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 By similarity. Some transportation to the nucleus when infected with C.jejeuni.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: MGI
    2. cell surface Source: MGI
    3. cytoplasm Source: RefGenome
    4. integral component of membrane Source: UniProtKB-KW
    5. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – 630610Mucin-1PRO_0000019280Add
    BLAST
    Chaini21 – 473453Mucin-1 subunit alphaBy similarityPRO_0000317452Add
    BLAST
    Chaini474 – 630157Mucin-1 subunit betaBy similarityPRO_0000317453Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi43 – 431O-linked (GalNAc...)Sequence Analysis
    Glycosylationi44 – 441O-linked (GalNAc...)Sequence Analysis
    Glycosylationi45 – 451O-linked (GalNAc...)Sequence Analysis
    Glycosylationi46 – 461O-linked (GalNAc...)Sequence Analysis
    Glycosylationi50 – 501O-linked (GalNAc...)Sequence Analysis
    Glycosylationi51 – 511O-linked (GalNAc...)Sequence Analysis
    Glycosylationi53 – 531O-linked (GalNAc...)Sequence Analysis
    Glycosylationi57 – 571O-linked (GalNAc...)Sequence Analysis
    Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi432 – 4321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence Analysis
    Lipidationi559 – 5591S-palmitoyl cysteineBy similarity
    Lipidationi561 – 5611S-palmitoyl cysteineBy similarity
    Modified residuei566 – 5661PhosphotyrosineBy similarity
    Modified residuei578 – 5781Phosphotyrosine; by PDGFRBy similarity
    Modified residuei584 – 5841PhosphotyrosineBy similarity
    Modified residuei587 – 5871PhosphotyrosineBy similarity
    Modified residuei593 – 5931Phosphotyrosine; by PDGFRBy similarity
    Modified residuei599 – 5991Phosphothreonine; by PKC/PRKCDBy similarity
    Modified residuei602 – 6021Phosphoserine; by GSK3-betaBy similarity
    Modified residuei604 – 6041Phosphotyrosine; by CSK, EGFR and SRCBy similarity
    Modified residuei618 – 6181PhosphotyrosineBy similarity

    Post-translational modificationi

    Probably both N- and extensively O-glycosylated (in repeat region).
    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.By similarity
    Dual palmitoylation on cysteine residues in the CQC motif is required for recycling from endosomes back to the plasma membrane.By similarity
    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.By similarity

    Keywords - PTMi

    Autocatalytic cleavage, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiQ02496.
    PRIDEiQ02496.

    PTM databases

    PhosphoSiteiQ02496.

    Expressioni

    Tissue specificityi

    Expressed in a variety of epithelial tissues.

    Gene expression databases

    BgeeiQ02496.
    CleanExiMM_MUC1.
    GenevestigatoriQ02496.

    Interactioni

    Subunit structurei

    The alpha subunit forms a tight, non-covalent heterodimeric complex with the proteolytically-released beta-subunit. 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 By similarity. C.jejeuni adheres to gastric epithelial MUC1 and modulates its transcription.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi201606. 1 interaction.
    STRINGi10090.ENSMUSP00000041963.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02496.
    SMRiQ02496. Positions 418-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 535515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini557 – 63074CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei536 – 55621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati42 – 61201Add
    BLAST
    Repeati62 – 81202Add
    BLAST
    Repeati82 – 101203Add
    BLAST
    Repeati102 – 122214; approximateAdd
    BLAST
    Repeati123 – 143215; approximateAdd
    BLAST
    Repeati144 – 164216; approximateAdd
    BLAST
    Repeati165 – 184207Add
    BLAST
    Repeati185 – 204208Add
    BLAST
    Repeati205 – 225219; approximateAdd
    BLAST
    Repeati226 – 2462110; approximateAdd
    BLAST
    Repeati247 – 2561011
    Repeati257 – 2863012Add
    BLAST
    Repeati287 – 3062013Add
    BLAST
    Repeati307 – 3262014Add
    BLAST
    Repeati327 – 3462015Add
    BLAST
    Repeati347 – 3662016Add
    BLAST
    Domaini416 – 521106SEAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 36632516 X 20 AA approximate tandem repeatsAdd
    BLAST
    Regioni567 – 60337Interaction with P53Add
    BLAST
    Regioni598 – 6058Required for interaction with GSK3BBy similarity
    Regioni608 – 6169Required for interaction with beta- and gamma-cateninsBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi578 – 5814Interaction with GRB2By similarity
    Motifi604 – 6074Interaction with SRC and ESR1By similarity
    Motifi618 – 6214Required for interaction with AP1S2By similarity

    Sequence similaritiesi

    Contains 1 SEA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG77744.
    GeneTreeiENSGT00710000106874.
    HOVERGENiHBG003075.
    InParanoidiQ02496.
    KOiK06568.
    OrthoDBiEOG7S7SFP.
    PhylomeDBiQ02496.
    TreeFamiTF336301.

    Family and domain databases

    Gene3Di3.30.70.960. 1 hit.
    InterProiIPR000082. SEA_dom.
    [Graphical view]
    PfamiPF01390. SEA. 1 hit.
    [Graphical view]
    SMARTiSM00200. SEA. 1 hit.
    [Graphical view]
    SUPFAMiSSF82671. SSF82671. 1 hit.
    PROSITEiPS50024. SEA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q02496-1 [UniParc]FASTAAdd to Basket

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    MTPGIRAPFF LLLLLASLKG FLALPSEENS VTSSQDTSSS LASTTTPVHS    50
    SNSDPATRPP GDSTSSPVQS STSSPATRAP EDSTSTAVLS GTSSPATTAP 100
    VNSASSPVAH GDTSSPATSL SKDSNSSPVV HSGTSSAATT APVDSTSSPV 150
    VHGGTSSPAT SPPGDSTSSP DHSSTSSPAT RAPEDSTSTA VLSGTSSPAT 200
    TAPVDSTSSP VAHDDTSSPA TSLSEDSASS PVAHGGTSSP ATSPLRDSTS 250
    SPVHSSASIQ NIKTTSDLAS TPDHNGTSVT TTSSALGSAT SPDHSGTSTT 300
    TNSSESVLAT TPVYSSMPFS TTKVTSGSAI IPDHNGSSVL PTSSVLGSAT 350
    SLVYNTSAIA TTPVSNGTQP SVPSQYPVSP TMATTSSHST IASSSYYSTV 400
    PFSTFSSNSS PQLSVGVSFF FLSFYIQNHP FNSSLEDPSS NYYQELKRNI 450
    SGLFLQIFNG DFLGISSIKF RSGSVVVEST VVFREGTFSA SDVKSQLIQH 500
    KKEADDYNLT ISEVKVNEMQ FPPSAQSRPG VPGWGIALLV LVCILVALAI 550
    VYFLALAVCQ CRRKSYGQLD IFPTQDTYHP MSEYPTYHTH GRYVPPGSTK 600
    RSPYEEVSAG NGSSSLSYTN PAVVTTSANL 630
    Length:630
    Mass (Da):64,539
    Last modified:February 5, 2008 - v2
    Checksum:iD9EC2A0815F65E8E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1212LS → PL in AAA39755. (PubMed:1714452)Curated
    Sequence conflicti138 – 1392AT → PA(PubMed:1958179)Curated
    Sequence conflicti140 – 1401T → TT(PubMed:1958179)Curated
    Sequence conflicti423 – 4231S → F in AAA39755. (PubMed:1714452)Curated
    Sequence conflicti506 – 5061D → S in AAA39755. (PubMed:1714452)Curated
    Sequence conflicti602 – 6021S → Q in AAA39755. (PubMed:1714452)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65132, M64928 Genomic DNA. Translation: AAA39755.1.
    M84683 mRNA. Translation: AAA39756.1.
    U16175 Genomic DNA. Translation: AAA98538.1.
    M77226 Genomic DNA. Translation: AAA39754.1.
    PIRiA39344.
    I52257.
    RefSeqiNP_038633.1. NM_013605.2.
    UniGeneiMm.16193.

    Genome annotation databases

    EnsembliENSMUST00000041142; ENSMUSP00000041963; ENSMUSG00000042784.
    GeneIDi17829.
    KEGGimmu:17829.
    UCSCiuc008pyh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65132 , M64928 Genomic DNA. Translation: AAA39755.1 .
    M84683 mRNA. Translation: AAA39756.1 .
    U16175 Genomic DNA. Translation: AAA98538.1 .
    M77226 Genomic DNA. Translation: AAA39754.1 .
    PIRi A39344.
    I52257.
    RefSeqi NP_038633.1. NM_013605.2.
    UniGenei Mm.16193.

    3D structure databases

    ProteinModelPortali Q02496.
    SMRi Q02496. Positions 418-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201606. 1 interaction.
    STRINGi 10090.ENSMUSP00000041963.

    Protein family/group databases

    MEROPSi S71.001.

    PTM databases

    PhosphoSitei Q02496.

    Proteomic databases

    PaxDbi Q02496.
    PRIDEi Q02496.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000041142 ; ENSMUSP00000041963 ; ENSMUSG00000042784 .
    GeneIDi 17829.
    KEGGi mmu:17829.
    UCSCi uc008pyh.1. mouse.

    Organism-specific databases

    CTDi 4582.
    MGIi MGI:97231. Muc1.

    Phylogenomic databases

    eggNOGi NOG77744.
    GeneTreei ENSGT00710000106874.
    HOVERGENi HBG003075.
    InParanoidi Q02496.
    KOi K06568.
    OrthoDBi EOG7S7SFP.
    PhylomeDBi Q02496.
    TreeFami TF336301.

    Enzyme and pathway databases

    Reactomei REACT_198517. O-linked glycosylation of mucins.
    REACT_198575. Termination of O-glycan biosynthesis.

    Miscellaneous databases

    NextBioi 292529.
    PROi Q02496.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q02496.
    CleanExi MM_MUC1.
    Genevestigatori Q02496.

    Family and domain databases

    Gene3Di 3.30.70.960. 1 hit.
    InterProi IPR000082. SEA_dom.
    [Graphical view ]
    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. "Molecular cloning and analysis of the mouse homologue of the tumor-associated mucin, MUC1, reveals conservation of potential O-glycosylation sites, transmembrane, and cytoplasmic domains and a loss of minisatellite-like polymorphism."
      Spicer A.P., Parry G., Patton S., Gendler S.J.
      J. Biol. Chem. 266:15099-15109(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The mouse episialin (Muc1) gene and its promoter: rapid evolution of the repetitive domain in the protein."
      Vos H.L., Devries Y., Hilkens J.
      Biochem. Biophys. Res. Commun. 181:121-130(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. Cited for: INTERACTION WITH CAMPYLOBACTER JEJUNI AND P53, INDUCTION, PHOSPHORYLATION.

    Entry informationi

    Entry nameiMUC1_MOUSE
    AccessioniPrimary (citable) accession number: Q02496
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    O-glycosylation sites are annotated in first sequence repeat only. Residues at similar position are probably glycosylated in all repeats.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3