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Q02496

- MUC1_MOUSE

UniProt

Q02496 - MUC1_MOUSE

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Protein

Mucin-1

Gene
Muc1, Muc-1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 autolysis By 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
Complete GO annotation...

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.
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 535515Extracellular Reviewed predictionAdd
BLAST
Transmembranei536 – 55621Helical; Reviewed predictionAdd
BLAST
Topological domaini557 – 63074Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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 alpha By similarityPRO_0000317452Add
BLAST
Chaini474 – 630157Mucin-1 subunit beta By similarityPRO_0000317453Add
BLAST

Amino acid modifications

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

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.1 Publication

Protein-protein interaction databases

BioGridi201606. 1 interaction.
STRINGi10090.ENSMUSP00000041963.

Structurei

3D structure databases

ProteinModelPortaliQ02496.
SMRiQ02496. Positions 418-473.

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 – 521106SEAAdd
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 GSK3B By similarity
Regioni608 – 6169Required for interaction with beta- and gamma-catenins By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi578 – 5814Interaction with GRB2 By similarity
Motifi604 – 6074Interaction with SRC and ESR1 By similarity
Motifi618 – 6214Required for interaction with AP1S2 By similarity

Sequence similaritiesi

Contains 1 SEA domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1212LS → PL in AAA39755. 1 Publication
Sequence conflicti138 – 1392AT → PA1 Publication
Sequence conflicti140 – 1401T → TT1 Publication
Sequence conflicti423 – 4231S → F in AAA39755. 1 Publication
Sequence conflicti506 – 5061D → S in AAA39755. 1 Publication
Sequence conflicti602 – 6021S → Q in AAA39755. 1 Publication

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: September 3, 2014
This is version 103 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.

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

Similar proteinsi