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P15941

- MUC1_HUMAN

UniProt

P15941 - MUC1_HUMAN

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Protein

Mucin-1

Gene

MUC1

Organism
Homo sapiens (Human)
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-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. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  3. transcription cofactor activity Source: BHF-UCL

GO - Biological processi

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

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 11581135ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1159 – 118123HelicalSequence AnalysisAdd
BLAST
Topological domaini1182 – 125574CytoplasmicSequence AnalysisAdd
BLAST

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: UniProtKB
  6. Golgi lumen Source: Reactome
  7. integral component of plasma membrane Source: ProtInc
  8. nuclear chromatin Source: BHF-UCL
  9. vesicle Source: UniProtKB
Complete GO annotation...

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. 1 Publication
Mutagenesisi1098 – 10981S → C or T: Almost complete cleavage. 1 Publication
Mutagenesisi1116 – 11161D → A: Greatly reduced formation of isoform 5/isoform Y complex. 1 Publication
Mutagenesisi1116 – 11161D → E: No effect on formation of isoform 5/isoform Y complex. 1 Publication
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. 1 Publication
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. 1 Publication
Mutagenesisi1187 – 11893RRK → AAA: No nuclear targeting of HRG-stimulated MUC1 C-terminal nor JUP/gamma-catenin. No effect on interaction with JUP/gamma-catenin. 2 Publications
Mutagenesisi1187 – 11893RRK → QQQ: No effect on palmitoylation. 2 Publications
Mutagenesisi1191 – 11911Y → F: No effect on EGFR-mediated phosphorylation. 2 Publications
Mutagenesisi1191 – 11911Y → N: No effect on endocytosis. 2 Publications
Mutagenesisi1203 – 12031Y → E: No effect on nuclear colocalization of MUC1CT and CTNNB1. No effect on in vitro PDFGR-induced cell invasiveness. 4 Publications
Mutagenesisi1203 – 12031Y → F: No effect on EGFR-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-induced cell invasiveness. 4 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. 4 Publications
Mutagenesisi1209 – 12091Y → F: Some reduction in EGFR-mediated phosphorylation. 1 Publication
Mutagenesisi1218 – 12181Y → F: No effect on EGFR-mediated phosphorylation. No nuclear colocalization of MUC1CT and CTNNB1. 2 Publications
Mutagenesisi1223 – 12231S → A: No change in PRKCD- nor GSK3B-mediated phosphorylation. 2 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. 1 Publication
Mutagenesisi1227 – 12271S → A: No change in PRKCD-mediated phosphorylation. Loss of GSK3B-mediated phosphorylation. CTNNB1. 2 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. 4 Publications
Mutagenesisi1229 – 12291Y → N: No effect on endocytosis. 4 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. 1 Publication

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

BgeeiP15941.
ExpressionAtlasiP15941. baseline and differential.
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
EGFRP005333EBI-2804728,EBI-297353
METP085812EBI-2804728,EBI-1039152
MUC1P15941-72EBI-2804728,EBI-4396776
U2AF2P263682EBI-2804728,EBI-742339

Protein-protein interaction databases

BioGridi110669. 32 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 – 105211Combined sources
Helixi1056 – 10594Combined sources
Helixi1064 – 108017Combined sources
Turni1082 – 10854Combined sources
Beta strandi1086 – 109611Combined sources
Beta strandi1099 – 11079Combined sources
Turni1109 – 11113Combined sources
Helixi1114 – 113219Combined sources
Beta strandi1136 – 11427Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00710000106874.
HOGENOMiHOG000290201.
HOVERGENiHBG003075.
InParanoidiP15941.
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

        10         20         30         40         50
MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE
60 70 80 90 100
KNAVSMTSSV LSSHSPGSGS STTQGQDVTL APATEPASGS AATWGQDVTS
110 120 130 140 150
VPVTRPALGS TTPPAHDVTS APDNKPAPGS TAPPAHGVTS APDTRPAPGS
160 170 180 190 200
TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
210 220 230 240 250
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS
260 270 280 290 300
TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
310 320 330 340 350
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS
360 370 380 390 400
TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
410 420 430 440 450
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS
460 470 480 490 500
TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
510 520 530 540 550
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS
560 570 580 590 600
TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
610 620 630 640 650
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS
660 670 680 690 700
TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
710 720 730 740 750
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS
760 770 780 790 800
TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
810 820 830 840 850
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS
860 870 880 890 900
TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS
910 920 930 940 950
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDNRPALGS
960 970 980 990 1000
TAPPVHNVTS ASGSASGSAS TLVHNGTSAR ATTTPASKST PFSIPSHHSD
1010 1020 1030 1040 1050
TPTTLASHST KTDASSTHHS SVPPLTSSNH STSPQLSTGV SFFFLSFHIS
1060 1070 1080 1090 1100
NLQFNSSLED PSTDYYQELQ RDISEMFLQI YKQGGFLGLS NIKFRPGSVV
1110 1120 1130 1140 1150
VQLTLAFREG TINVHDVETQ FNQYKTEAAS RYNLTISDVS VSDVPFPFSA
1160 1170 1180 1190 1200
QSGAGVPGWG IALLVLVCVL VALAIVYLIA LAVCQCRRKN YGQLDIFPAR
1210 1220 1230 1240 1250
DTYHPMSEYP TYHTHGRYVP PSSTDRSPYE KVSAGNGGSS LSYTNPAVAA

TSANL
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.Curated
The sequence AAD14376.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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]
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]
ENST00000620103; ENSP00000481231; ENSG00000185499.
GeneIDi4582.
KEGGihsa:4582.
UCSCiuc001fia.3. human. [P15941-7]
uc001fib.3. human. [P15941-10]
uc001fid.3. human.
uc001fie.3. human. [P15941-9]
uc001fig.3. human.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 32 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 ]
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 ]
ENST00000620103 ; ENSP00000481231 ; ENSG00000185499 .
GeneIDi 4582.
KEGGi hsa:4582.
UCSCi uc001fia.3. human. [P15941-7 ]
uc001fib.3. human. [P15941-10 ]
uc001fid.3. human.
uc001fie.3. human. [P15941-9 ]
uc001fig.3. human.
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.
GeneTreei ENSGT00710000106874.
HOGENOMi HOG000290201.
HOVERGENi HBG003075.
InParanoidi P15941.
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

Bgeei P15941.
ExpressionAtlasi P15941. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 168 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