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Protein

Mucin-1

Gene

MUC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

  • p53 binding Source: BHF-UCL
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  • transcription cofactor activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-5083625. Defective GALNT3 causes familial hyperphosphatemic tumoral calcinosis (HFTC).
R-HSA-5083632. Defective C1GALT1C1 causes Tn polyagglutination syndrome (TNPS).
R-HSA-5083636. Defective GALNT12 causes colorectal cancer 1 (CRCS1).
R-HSA-913709. O-linked glycosylation of mucins.
R-HSA-977068. Termination of O-glycan biosynthesis.
SIGNORiP15941.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7508. MUC1.

Subcellular locationi

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)DescriptionActionsGraphical viewLength
Topological domaini24 – 1158ExtracellularSequence analysisAdd BLAST1135
Transmembranei1159 – 1181HelicalSequence analysisAdd BLAST23
Topological domaini1182 – 1255CytoplasmicSequence analysisAdd BLAST74

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi lumen Source: Reactome
  • integral component of plasma membrane Source: ProtInc
  • nuclear chromatin Source: BHF-UCL
  • 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.

Medullary cystic kidney disease 1 (MCKD1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:174000

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1098S → A, D, E, F, G, H, I, K, L, M, N, P, Q, R, V, W or Y: Completely abrogates cleavage. 1 Publication1
Mutagenesisi1098S → C or T: Almost complete cleavage. 1 Publication1
Mutagenesisi1116D → A: Greatly reduced formation of isoform 5/isoform Y complex. 1 Publication1
Mutagenesisi1116D → E: No effect on formation of isoform 5/isoform Y complex. 1 Publication1
Mutagenesisi1184C → 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 Publication1
Mutagenesisi1186C → 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 Publication1
Mutagenesisi1187 – 1189RRK → AAA: No nuclear targeting of HRG-stimulated MUC1 C-terminal nor JUP/gamma-catenin. No effect on interaction with JUP/gamma-catenin. 2 Publications3
Mutagenesisi1187 – 1189RRK → QQQ: No effect on palmitoylation. 2 Publications3
Mutagenesisi1191Y → F: No effect on EGFR-mediated phosphorylation. 2 Publications1
Mutagenesisi1191Y → N: No effect on endocytosis. 2 Publications1
Mutagenesisi1203Y → E: No effect on nuclear colocalization of MUC1CT and CTNNB1. No effect on in vitro PDFGR-induced cell invasiveness. 4 Publications1
Mutagenesisi1203Y → F: No effect on EGFR-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-induced cell invasiveness. 4 Publications1
Mutagenesisi1203Y → 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 Publications1
Mutagenesisi1209Y → F: Some reduction in EGFR-mediated phosphorylation. 1 Publication1
Mutagenesisi1218Y → F: No effect on EGFR-mediated phosphorylation. No nuclear colocalization of MUC1CT and CTNNB1. 2 Publications1
Mutagenesisi1223S → A: No change in PRKCD- nor GSK3B-mediated phosphorylation. 2 Publications1
Mutagenesisi1224T → 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 Publication1
Mutagenesisi1227S → A: No change in PRKCD-mediated phosphorylation. Loss of GSK3B-mediated phosphorylation. CTNNB1. 2 Publications1
Mutagenesisi1229Y → F: Greatly reduced EGFR- and Src-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-mediated phosphorylation. Decreased Src-binding. 4 Publications1
Mutagenesisi1229Y → N: No effect on endocytosis. 4 Publications1
Mutagenesisi1243Y → 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 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi4582.
MalaCardsiMUC1.
MIMi174000. phenotype.
OpenTargetsiENSG00000185499.
Orphaneti34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
PharmGKBiPA31309.

Chemistry databases

ChEMBLiCHEMBL3580494.

Polymorphism and mutation databases

BioMutaiMUC1.
DMDMi296439295.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 232 PublicationsAdd BLAST23
ChainiPRO_000001927724 – 1255Mucin-1Add BLAST1232
ChainiPRO_000031744624 – 1097Mucin-1 subunit alphaAdd BLAST1074
ChainiPRO_00003174471098 – 1255Mucin-1 subunit betaAdd BLAST158

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi131O-linked (GalNAc...)2 Publications1
Glycosylationi139O-linked (GalNAc...)2 Publications1
Glycosylationi140O-linked (GalNAc...)Sequence analysis1
Glycosylationi144O-linked (GalNAc...)Sequence analysis1
Glycosylationi957N-linked (GlcNAc...)Sequence analysis1
Glycosylationi975N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1029N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1055N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1133N-linked (GlcNAc...)Sequence analysis1
Lipidationi1184S-palmitoyl cysteine1 Publication1
Lipidationi1186S-palmitoyl cysteine1 Publication1
Modified residuei1203Phosphotyrosine; by PDGFR2 Publications1
Modified residuei1212Phosphotyrosine1 Publication1
Modified residuei1218Phosphotyrosine; by PDGFR1 Publication1
Modified residuei1224Phosphothreonine; by PKC/PRKCD1 Publication1
Modified residuei1227Phosphoserine; by GSK3-betaCombined sources1 Publication1
Modified residuei1229Phosphotyrosine; by CSK, EGFR and SRC4 Publications1
Modified residuei1243Phosphotyrosine1 Publication1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1097 – 1098Cleavage; by autolysis2

Keywords - PTMi

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

Proteomic databases

MaxQBiP15941.
PaxDbiP15941.
PeptideAtlasiP15941.
PRIDEiP15941.

PTM databases

iPTMnetiP15941.
PhosphoSitePlusiP15941.
SwissPalmiP15941.
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 Y 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

BgeeiENSG00000185499.
ExpressionAtlasiP15941. baseline and differential.
GenevisibleiP15941. HS.

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
CEBPBP176768EBI-10053698,EBI-969696
EGFRP005333EBI-2804728,EBI-297353
METP085812EBI-2804728,EBI-1039152
MUC1P15941-72EBI-2804728,EBI-4396776
U2AF2P263682EBI-2804728,EBI-742339

GO - Molecular functioni

  • p53 binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110669. 42 interactors.
DIPiDIP-41890N.
IntActiP15941. 9 interactors.
MINTiMINT-156679.
STRINGi9606.ENSP00000357380.

Structurei

Secondary structure

11255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1042 – 1052Combined sources11
Helixi1056 – 1059Combined sources4
Helixi1064 – 1080Combined sources17
Turni1082 – 1085Combined sources4
Beta strandi1086 – 1096Combined sources11
Beta strandi1099 – 1107Combined sources9
Turni1109 – 1111Combined sources3
Helixi1114 – 1132Combined sources19
Beta strandi1136 – 1142Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SM3X-ray1.95P919-931[»]
2ACMNMR-A1042-1097[»]
B1098-1152[»]
2FO4X-ray2.70P140-146[»]
ProteinModelPortaliP15941.
SMRiP15941.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15941.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati61 – 801; approximate1 PublicationAdd BLAST20
Repeati81 – 1002; approximate1 PublicationAdd BLAST20
Repeati101 – 12031 PublicationAdd BLAST20
Repeati121 – 14041 PublicationAdd BLAST20
Repeati141 – 16051 PublicationAdd BLAST20
Repeati161 – 18061 PublicationAdd BLAST20
Repeati181 – 20071 PublicationAdd BLAST20
Repeati201 – 22081 PublicationAdd BLAST20
Repeati221 – 24091 PublicationAdd BLAST20
Repeati241 – 260101 PublicationAdd BLAST20
Repeati261 – 280111 PublicationAdd BLAST20
Repeati281 – 300121 PublicationAdd BLAST20
Repeati301 – 320131 PublicationAdd BLAST20
Repeati321 – 340141 PublicationAdd BLAST20
Repeati341 – 360151 PublicationAdd BLAST20
Repeati361 – 380161 PublicationAdd BLAST20
Repeati381 – 400171 PublicationAdd BLAST20
Repeati401 – 420181 PublicationAdd BLAST20
Repeati421 – 440191 PublicationAdd BLAST20
Repeati441 – 460201 PublicationAdd BLAST20
Repeati461 – 480211 PublicationAdd BLAST20
Repeati481 – 500221 PublicationAdd BLAST20
Repeati501 – 520231 PublicationAdd BLAST20
Repeati521 – 540241 PublicationAdd BLAST20
Repeati541 – 560251 PublicationAdd BLAST20
Repeati561 – 580261 PublicationAdd BLAST20
Repeati581 – 600271 PublicationAdd BLAST20
Repeati601 – 620281 PublicationAdd BLAST20
Repeati621 – 640291 PublicationAdd BLAST20
Repeati641 – 660301 PublicationAdd BLAST20
Repeati661 – 680311 PublicationAdd BLAST20
Repeati681 – 700321 PublicationAdd BLAST20
Repeati701 – 720331 PublicationAdd BLAST20
Repeati721 – 740341 PublicationAdd BLAST20
Repeati741 – 760351 PublicationAdd BLAST20
Repeati761 – 780361 PublicationAdd BLAST20
Repeati781 – 800371 PublicationAdd BLAST20
Repeati801 – 820381 PublicationAdd BLAST20
Repeati821 – 840391 PublicationAdd BLAST20
Repeati841 – 860401 PublicationAdd BLAST20
Repeati861 – 880411 PublicationAdd BLAST20
Repeati881 – 900421 PublicationAdd BLAST20
Repeati901 – 920431 PublicationAdd BLAST20
Repeati921 – 940441 PublicationAdd BLAST20
Repeati941 – 960451 PublicationAdd BLAST20
Repeati961 – 98046; approximate1 PublicationAdd BLAST20
Repeati981 – 100047; approximate1 PublicationAdd BLAST20
Repeati1001 – 102048; approximate1 PublicationAdd BLAST20
Domaini1039 – 1148SEAPROSITE-ProRule annotationAdd BLAST110

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 96542 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 BLAST840
Regioni1192 – 1228Interaction with P53Add BLAST37
Regioni1223 – 1230Required for interaction with GSK3B8
Regioni1233 – 1241Required for interaction with beta- and gamma-catenins9

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1203 – 1206Interaction with GRB24
Motifi1229 – 1232Interaction with SRC and ESR14
Motifi1243 – 1246Required for interaction with AP1S24

Sequence similaritiesi

Contains 1 SEA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IX6R. Eukaryota.
ENOG410ZQ7Z. LUCA.
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:SF8. PTHR10006:SF8. 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. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2T → A in AAD14369 (PubMed:8604237).Curated1
Sequence conflicti134P → Q in AAA35757 (PubMed:2597151).Curated1
Sequence conflicti154P → Q in AAA35757 (PubMed:2597151).Curated1
Sequence conflicti1021S → T in AAA35805 (PubMed:2318825).Curated1
Sequence conflicti1021S → T in AAA35807 (PubMed:2318825).Curated1
Sequence conflicti1021S → T in AAA59876 (PubMed:1697589).Curated1
Sequence conflicti1143D → G in AAP97018 (PubMed:22941036).Curated1
Sequence conflicti1193Q → L in AAK30142 (PubMed:15969018).Curated1
Sequence conflicti1231K → T in AAD10858 (PubMed:9212228).Curated1
Sequence conflicti1251T → A in AAA60019 (PubMed:2394722).Curated1

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_0193901117V → M.3 PublicationsCorresponds to variant rs1611770dbSNPEnsembl.1
Natural variantiVAR_0193911142S → N.1 PublicationCorresponds to variant rs11465207dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00328119 – 21Missing in isoform 3. 1 Publication3
Alternative sequenceiVSP_00328019T → TATTAPKPAT in isoform 2, isoform Y-LSP, isoform E2, isoform J13, isoform S2 and isoform T10. 6 Publications1
Alternative sequenceiVSP_00328220 – 31Missing in isoform 4. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_04787254 – 1151Missing in isoform E2. 1 PublicationAdd BLAST1098
Alternative sequenceiVSP_04787354 – 1093Missing in isoform T10. 1 PublicationAdd BLAST1040
Alternative sequenceiVSP_00328554 – 1053Missing in isoform J13, isoform Y, isoform Y-LSP and isoform S2. 6 PublicationsAdd BLAST1000
Alternative sequenceiVSP_00328654 – 1035Missing in isoform 8, isoform 9 and isoform M6. 4 PublicationsAdd BLAST982
Alternative sequenceiVSP_04757554 – 96VSMTS…ATWGQ → IPAPTTTKSCRETFLKCFCR FINKGVFWASPILSSGQDLW WYN in isoform ZD. 2 PublicationsAdd BLAST43
Alternative sequenceiVSP_03504654 – 87VSMTS…ATEPA → IPAPTTTKSCRETFLKCFCR FINKGVFWASPILS in isoform F. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_00328354 – 70VSMTS…PGSGS → IPAPTTTKSCRETFLKW in isoform 6. 2 PublicationsAdd BLAST17
Alternative sequenceiVSP_00328471 – 1095Missing in isoform 6. 2 PublicationsAdd BLAST1025
Alternative sequenceiVSP_03504788 – 1139Missing in isoform F. 1 PublicationAdd BLAST1052
Alternative sequenceiVSP_04757697 – 1255Missing in isoform ZD. 2 PublicationsAdd BLAST1159
Alternative sequenceiVSP_0032871077 – 1181Missing in isoform 9 and isoform S2. 3 PublicationsAdd BLAST105
Alternative sequenceiVSP_0032881077 – 1087FLQIYKQGGFL → VSIGLSFPMLP in isoform 5. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_0032891088 – 1255Missing in isoform 5. 1 PublicationAdd BLAST168
Alternative sequenceiVSP_0469621141 – 1180VSDVP…VYLIA → GCLSVPPKELRAAGHLSSPG YLPSYERVPHLPHPWALCAP in isoform M6. 2 PublicationsAdd BLAST40
Alternative sequenceiVSP_0469631181 – 1255Missing in isoform M6. 2 PublicationsAdd BLAST75
Alternative sequenceiVSP_0478741232 – 1255VSAGN…TSANL → RQNGWSTMPRGALPEESQG in isoform J13. 1 PublicationAdd BLAST24

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]
GeneIDi4582.
KEGGihsa:4582.
UCSCiuc001fia.4. human. [P15941-1]

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SM3X-ray1.95P919-931[»]
2ACMNMR-A1042-1097[»]
B1098-1152[»]
2FO4X-ray2.70P140-146[»]
ProteinModelPortaliP15941.
SMRiP15941.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110669. 42 interactors.
DIPiDIP-41890N.
IntActiP15941. 9 interactors.
MINTiMINT-156679.
STRINGi9606.ENSP00000357380.

Chemistry databases

ChEMBLiCHEMBL3580494.

Protein family/group databases

MEROPSiS71.001.

PTM databases

iPTMnetiP15941.
PhosphoSitePlusiP15941.
SwissPalmiP15941.
UniCarbKBiP15941.

Polymorphism and mutation databases

BioMutaiMUC1.
DMDMi296439295.

Proteomic databases

MaxQBiP15941.
PaxDbiP15941.
PeptideAtlasiP15941.
PRIDEiP15941.

Protocols and materials databases

DNASUi4582.
Structural Biology KnowledgebaseSearch...

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]
GeneIDi4582.
KEGGihsa:4582.
UCSCiuc001fia.4. human. [P15941-1]

Organism-specific databases

CTDi4582.
DisGeNETi4582.
GeneCardsiMUC1.
GeneReviewsiMUC1.
HGNCiHGNC:7508. MUC1.
HPAiCAB000036.
CAB001986.
HPA004179.
HPA007235.
HPA008855.
MalaCardsiMUC1.
MIMi113720. gene.
158340. gene.
174000. phenotype.
neXtProtiNX_P15941.
OpenTargetsiENSG00000185499.
Orphaneti34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
PharmGKBiPA31309.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IX6R. Eukaryota.
ENOG410ZQ7Z. LUCA.
GeneTreeiENSGT00710000106874.
HOGENOMiHOG000290201.
HOVERGENiHBG003075.
InParanoidiP15941.
KOiK06568.
PhylomeDBiP15941.

Enzyme and pathway databases

ReactomeiR-HSA-5083625. Defective GALNT3 causes familial hyperphosphatemic tumoral calcinosis (HFTC).
R-HSA-5083632. Defective C1GALT1C1 causes Tn polyagglutination syndrome (TNPS).
R-HSA-5083636. Defective GALNT12 causes colorectal cancer 1 (CRCS1).
R-HSA-913709. O-linked glycosylation of mucins.
R-HSA-977068. Termination of O-glycan biosynthesis.
SIGNORiP15941.

Miscellaneous databases

ChiTaRSiMUC1. human.
EvolutionaryTraceiP15941.
GeneWikiiMUC1.
GenomeRNAii4582.
PROiP15941.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185499.
ExpressionAtlasiP15941. baseline and differential.
GenevisibleiP15941. HS.

Family and domain databases

Gene3Di3.30.70.960. 1 hit.
InterProiIPR023217. Mucin-1.
IPR000082. SEA_dom.
[Graphical view]
PANTHERiPTHR10006:SF8. PTHR10006:SF8. 1 hit.
PfamiPF01390. SEA. 1 hit.
[Graphical view]
SMARTiSM00200. SEA. 1 hit.
[Graphical view]
SUPFAMiSSF82671. SSF82671. 1 hit.
PROSITEiPS50024. SEA. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 191 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.

Caution

O-glycosylation sites are annotated in first sequence repeat only. Residues at similar position are probably glycosylated in all repeats. Experimental sites were determined in a synthetic peptide glycosylated in vitro (PubMed:7744025, PubMed:9597769).2 Publications

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.