P15941 (MUC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mucin-1
Short name=MUC-1

Alternative name(s):
Breast carcinoma-associated antigen DF3
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:

1. Mucin-1 subunit alpha
   Short name=MUC1-NT
   Short name=MUC1-alpha
2. Mucin-1 subunit beta
   Short name=MUC1-beta
   Alternative name(s):
   MUC1-CT

Gene names

Name:	MUC1
Synonyms:	PUM

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1255 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.26 Ref.37 Ref.40 Ref.45 Ref.46 Ref.49 Ref.52 Ref.53 Ref.56 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. Ref.26 Ref.37 Ref.40 Ref.45 Ref.46 Ref.49 Ref.52 Ref.53 Ref.56
Subunit structure	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. Ref.24 Ref.26 Ref.30 Ref.32 Ref.34 Ref.36 Ref.37 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.56
Subcellular location	Apical cell membrane; Single-pass type I membrane protein. Note: Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized and recycled to the cell membrane. Located to microvilli and to the tips of long filopodial protusions. Ref.33 Ref.42 Ref.43 Ref.44 Ref.48 Ref.50 Ref.52 Ref.54 Isoform 5: Secreted Ref.33 Ref.42 Ref.43 Ref.44 Ref.48 Ref.50 Ref.52 Ref.54. Isoform 7: Secreted Ref.33 Ref.42 Ref.43 Ref.44 Ref.48 Ref.50 Ref.52 Ref.54. Isoform 9: Secreted Ref.33 Ref.42 Ref.43 Ref.44 Ref.48 Ref.50 Ref.52 Ref.54. 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. Ref.33 Ref.42 Ref.43 Ref.44 Ref.48 Ref.50 Ref.52 Ref.54
Tissue specificity	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. Ref.9 Ref.49
Developmental stage	During fetal development, expressed at low levels in the colonic epithelium from 13 weeks of gestation. Ref.28
Post-translational modification	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. Ref.22 Ref.25 Ref.27 Ref.29 Ref.48 Ref.57 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. Dual palmitoylation on cysteine residues in the CQC motif is required for recycling from endosomes back to the plasma membrane. 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. Ref.23 Ref.24 Ref.30 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.46 Ref.49 Ref.54 Ref.55 The N-terminal sequence has been shown to begin at position 24 or 28 (Ref.20).
Polymorphism	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.
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.
Sequence similarities	Contains 1 SEA domain.
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 (Ref.25, Ref.29).
Sequence caution	The sequence AAD14369.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAD14376.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	Repeat Signal Transmembrane Transmembrane helix
PTM	Autocatalytic cleavage Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	apical plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome cell surface Inferred from Biological aspect of Ancestor. Source: RefGenome cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MUC1	P15941-7	2	EBI-2804728,EBI-4396776

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P15941-1)

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.

Isoform 2 (identifier: P15941-2)

Also known as: B;

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

Isoform 3 (identifier: P15941-3)

Also known as: C;

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

Isoform 4 (identifier: P15941-4)

Also known as: D;

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

Isoform 5 (identifier: P15941-5)

Also known as: SEC;

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

Isoform 6 (identifier: P15941-6)

Also known as: X;

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

Isoform 7 (identifier: P15941-7)

Also known as: Y;

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

Isoform 8 (identifier: P15941-8)

Also known as: Z;

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

Isoform 9 (identifier: P15941-9)

Also known as: S;

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

Isoform 10 (identifier: P15941-10)

Also known as: F;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.20

Chain

24 – 1255

1232

Mucin-1

PRO_0000019277

Chain

24 – 1097

1074

Mucin-1 subunit alpha

PRO_0000317446

Chain

1098 – 1255

158

Mucin-1 subunit beta

PRO_0000317447

Regions

Topological domain

24 – 1158

1135

Extracellular Potential

Transmembrane

1159 – 1181

23

Helical; Potential

Topological domain

1182 – 1255

74

Cytoplasmic Potential

Repeat

61 – 80

20

1; approximate

Repeat

81 – 100

20

2; approximate

Repeat

101 – 120

20

3

Repeat

121 – 140

20

4

Repeat

141 – 160

20

5

Repeat

161 – 180

20

6

Repeat

181 – 200

20

7

Repeat

201 – 220

20

8

Repeat

221 – 240

20

9

Repeat

241 – 260

20

10

Repeat

261 – 280

20

11

Repeat

281 – 300

20

12

Repeat

301 – 320

20

13

Repeat

321 – 340

20

14

Repeat

341 – 360

20

15

Repeat

361 – 380

20

16

Repeat

381 – 400

20

17

Repeat

401 – 420

20

18

Repeat

421 – 440

20

19

Repeat

441 – 460

20

20

Repeat

461 – 480

20

21

Repeat

481 – 500

20

22

Repeat

501 – 520

20

23

Repeat

521 – 540

20

24

Repeat

541 – 560

20

25

Repeat

561 – 580

20

26

Repeat

581 – 600

20

27

Repeat

601 – 620

20

28

Repeat

621 – 640

20

29

Repeat

641 – 660

20

30

Repeat

661 – 680

20

31

Repeat

681 – 700

20

32

Repeat

701 – 720

20

33

Repeat

721 – 740

20

34

Repeat

741 – 760

20

35

Repeat

761 – 780

20

36

Repeat

781 – 800

20

37

Repeat

801 – 820

20

38

Repeat

821 – 840

20

39

Repeat

841 – 860

20

40

Repeat

861 – 880

20

41

Repeat

881 – 900

20

42

Repeat

901 – 920

20

43

Repeat

921 – 940

20

44

Repeat

941 – 960

20

45

Repeat

961 – 980

20

46; approximate

Repeat

981 – 1000

20

47; approximate

Repeat

1001 – 1020

20

48; approximate

Domain

1034 – 1151

118

SEA

Region

126 – 965

840

42 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-R

Region

1192 – 1228

37

Interaction with P53

Region

1223 – 1230

8

Required for interaction with GSK3B

Region

1233 – 1241

9

Required for interaction with beta- and gamma-catenins

Motif

1203 – 1206

4

Interaction with GRB2

Motif

1229 – 1232

4

Interaction with SRC and ESR1

Motif

1243 – 1246

4

Required for interaction with AP1S2

Sites

Site

1097 – 1098

2

Cleavage; by autolysis

Amino acid modifications

Modified residue

1191

1

Phosphotyrosine Ref.55

Modified residue

1203

1

Phosphotyrosine; by PDGFR Ref.38 Ref.54 Ref.55

Modified residue

1209

1

Phosphotyrosine Ref.55

Modified residue

1212

1

Phosphotyrosine Ref.38 Ref.55

Modified residue

1218

1

Phosphotyrosine; by PDGFR Ref.54 Ref.55

Modified residue

1224

1

Phosphothreonine; by PKC/PRKCD Ref.37

Modified residue

1227

1

Phosphoserine; by GSK3-beta Ref.30

Modified residue

1229

1

Phosphotyrosine; by CSK, EGFR and SRC Ref.34 Ref.36 Ref.38 Ref.54 Ref.55

Modified residue

1243

1

Phosphotyrosine Ref.38 Ref.55

Lipidation

1184

1

S-palmitoyl cysteine Ref.50

Lipidation

1186

1

S-palmitoyl cysteine Ref.50

Glycosylation

131

1

O-linked (GalNAc...) Probable

Glycosylation

139

1

O-linked (GalNAc...) Probable

Glycosylation

140

1

O-linked (GalNAc...) Potential

Glycosylation

144

1

O-linked (GalNAc...) Potential

Glycosylation

957

1

N-linked (GlcNAc...) Potential

Glycosylation

975

1

N-linked (GlcNAc...) Potential

Glycosylation

1029

1

N-linked (GlcNAc...) Potential

Glycosylation

1055

1

N-linked (GlcNAc...) Potential

Glycosylation

1133

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

19 – 21

3

Missing in isoform 3.

VSP_003281

Alternative sequence

19

1

T → TATTAPKPAT in isoform 2.

VSP_003280

Alternative sequence

20 – 31

12

Missing in isoform 4.

VSP_003282

Alternative sequence

54 – 1053

1000

Missing in isoform 7.

VSP_003285

Alternative sequence

54 – 1035

982

Missing in isoform 8 and isoform 9.

VSP_003286

Alternative sequence

54 – 87

34

VSMTS…ATEPA → IPAPTTTKSCRETFLKCFCR FINKGVFWASPILS in isoform 10.

VSP_035046

Alternative sequence

54 – 70

17

VSMTS…PGSGS → IPAPTTTKSCRETFLKW in isoform 6.

VSP_003283

Alternative sequence

71 – 1095

1025

Missing in isoform 6.

VSP_003284

Alternative sequence

88 – 1139

1052

Missing in isoform 10.

VSP_035047

Alternative sequence

1077 – 1181

105

Missing in isoform 9.

VSP_003287

Alternative sequence

1077 – 1087

11

FLQIYKQGGFL → VSIGLSFPMLP in isoform 5.

VSP_003288

Alternative sequence

1088 – 1255

168

Missing in isoform 5.

VSP_003289

Natural variant

1117

1

V → M. Ref.11 Ref.13
Corresponds to variant rs1611770 [ dbSNP | Ensembl ].

VAR_019390

Natural variant

1142

1

S → N. Ref.13
Corresponds to variant rs11465207 [ dbSNP | Ensembl ].

VAR_019391

Experimental info

Mutagenesis

1098

1

S → A, D, E, F, G, H, I, K, L, M, N, P, Q, R, V, W or Y: Completely abrogates cleavage. Ref.21

Mutagenesis

1098

1

S → C or T: Almost complete cleavage. Ref.21

Mutagenesis

1116

1

D → A: Greatly reduced formation of isoform 5/isoform 7 complex. Ref.31

Mutagenesis

1116

1

D → E: No effect on formation of isoform 5/isoform 7 complex. Ref.31

Mutagenesis

1184

1

C → 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. Ref.50

Mutagenesis

1186

1

C → 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. Ref.50

Mutagenesis

1187 – 1189

3

RRK → AAA: No nuclear targeting of HRG-stimulated MUC1 C-terminal nor JUP/gamma-catenin. No effect on interaction with JUP/gamma-catenin. Ref.43 Ref.50

Mutagenesis

1187 – 1189

3

RRK → QQQ: No effect on palmitoylation. Ref.43 Ref.50

Mutagenesis

1191

1

Y → F: No effect on EGFR-mediated phosphorylation. Ref.36 Ref.44

Mutagenesis

1191

1

Y → N: No effect on endocytosis. Ref.36 Ref.44

Mutagenesis

1203

1

Y → E: No effect on nuclear colocalization of MUC1CT and CTNNB1. No effect on in vitro PDFGR-induced cell invasiveness. Ref.36 Ref.44 Ref.50 Ref.54

Mutagenesis

1203

1

Y → F: No effect on EGFR-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-induced cell invasiveness. Ref.36 Ref.44 Ref.50 Ref.54

Mutagenesis

1203

1

Y → 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. Ref.36 Ref.44 Ref.50 Ref.54

Mutagenesis

1209

1

Y → F: Some reduction in EGFR-mediated phosphorylation. Ref.36

Mutagenesis

1218

1

Y → F: No effect on EGFR-mediated phosphorylation. No nuclear colocalization of MUC1CT and CTNNB1. Ref.36 Ref.54

Mutagenesis

1223

1

S → A: No change in PRKCD- nor GSK3B-mediated phosphorylation. Ref.30 Ref.37

Mutagenesis

1224

1

T → 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. Ref.37

Mutagenesis

1227

1

S → A: No change in PRKCD-mediated phosphorylation. Loss of GSK3B-mediated phosphorylation. CTNNB1. Ref.30 Ref.37

Mutagenesis

1229

1

Y → F: Greatly reduced EGFR- and Src-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-mediated phosphorylation. Decreased Src-binding. Ref.34 Ref.36 Ref.40 Ref.44

Mutagenesis

1229

1

Y → N: No effect on endocytosis. Ref.34 Ref.36 Ref.40 Ref.44

Mutagenesis

1243

1

Y → 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. Ref.44

Sequence conflict

2

1

T → A in AAD14369. Ref.18

Sequence conflict

134

1

P → Q in AAA35757. Ref.16

Sequence conflict

154

1

P → Q Ref.16

Sequence conflict

1021

1

S → T Ref.2

Sequence conflict

1021

1

S → T Ref.3

Sequence conflict

1193

1

Q → L in AAK30142. Ref.11

Sequence conflict

1231

1

K → T in AAD10858. Ref.9

Sequence conflict

1251

1

T → A in AAA60019. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1255

Helix Strand Turn

Details...

Beta strand

1042 – 1052

11

Helix

1056 – 1059

4

Helix

1064 – 1080

17

Turn

1082 – 1085

4

Beta strand

1086 – 1096

11

Beta strand

1099 – 1107

9

Turn

1109 – 1111

3

Helix

1114 – 1132

19

Beta strand

1136 – 1142

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 5E28DFC4C20D9A82	FASTA	1,255	122,102
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNAVSMTSSV 70 80 90 100 110 120 LSSHSPGSGS STTQGQDVTL APATEPASGS AATWGQDVTS VPVTRPALGS TTPPAHDVTS 130 140 150 160 170 180 APDNKPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 190 200 210 220 230 240 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 250 260 270 280 290 300 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 310 320 330 340 350 360 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 370 380 390 400 410 420 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 430 440 450 460 470 480 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 490 500 510 520 530 540 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 550 560 570 580 590 600 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 610 620 630 640 650 660 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 670 680 690 700 710 720 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 730 740 750 760 770 780 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 790 800 810 820 830 840 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 850 860 870 880 890 900 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 910 920 930 940 950 960 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDNRPALGS TAPPVHNVTS 970 980 990 1000 1010 1020 ASGSASGSAS TLVHNGTSAR ATTTPASKST PFSIPSHHSD TPTTLASHST KTDASSTHHS 1030 1040 1050 1060 1070 1080 SVPPLTSSNH STSPQLSTGV SFFFLSFHIS NLQFNSSLED PSTDYYQELQ RDISEMFLQI 1090 1100 1110 1120 1130 1140 YKQGGFLGLS NIKFRPGSVV VQLTLAFREG TINVHDVETQ FNQYKTEAAS RYNLTISDVS 1150 1160 1170 1180 1190 1200 VSDVPFPFSA QSGAGVPGWG IALLVLVCVL VALAIVYLIA LAVCQCRRKN YGQLDIFPAR 1210 1220 1230 1240 1250 DTYHPMSEYP TYHTHGRYVP PSSTDRSPYE KVSAGNGGSS LSYTNPAVAA TSANL
	Isoform 2 (B) [UniParc]. Checksum: 3810149471D221FD	FASTA	1,264	122,941
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTA TTAPKPATVV TGSGHASSTP GGEKETSATQ RSSVPSSTEK 70 80 90 100 110 120 NAVSMTSSVL SSHSPGSGSS TTQGQDVTLA PATEPASGSA ATWGQDVTSV PVTRPALGST 130 140 150 160 170 180 TPPAHDVTSA PDNKPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 190 200 210 220 230 240 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 250 260 270 280 290 300 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 310 320 330 340 350 360 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 370 380 390 400 410 420 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 430 440 450 460 470 480 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 490 500 510 520 530 540 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 550 560 570 580 590 600 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 610 620 630 640 650 660 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 670 680 690 700 710 720 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 730 740 750 760 770 780 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 790 800 810 820 830 840 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 850 860 870 880 890 900 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST 910 920 930 940 950 960 APPAHGVTSA PDTRPAPGST APPAHGVTSA PDTRPAPGST APPAHGVTSA PDNRPALGST 970 980 990 1000 1010 1020 APPVHNVTSA SGSASGSAST LVHNGTSARA TTTPASKSTP FSIPSHHSDT PTTLASHSTK 1030 1040 1050 1060 1070 1080 TDASSTHHSS VPPLTSSNHS TSPQLSTGVS FFFLSFHISN LQFNSSLEDP STDYYQELQR 1090 1100 1110 1120 1130 1140 DISEMFLQIY KQGGFLGLSN IKFRPGSVVV QLTLAFREGT INVHDVETQF NQYKTEAASR 1150 1160 1170 1180 1190 1200 YNLTISDVSV SDVPFPFSAQ SGAGVPGWGI ALLVLVCVLV ALAIVYLIAL AVCQCRRKNY 1210 1220 1230 1240 1250 1260 GQLDIFPARD TYHPMSEYPT YHTHGRYVPP SSTDRSPYEK VSAGNGGSSL SYTNPAVAAT SANL
	Isoform 3 (C) [UniParc]. Checksum: A3F30DBFE56DD0C5	FASTA	1,252	121,803
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTG SGHASSTPGG EKETSATQRS SVPSSTEKNA VSMTSSVLSS 70 80 90 100 110 120 HSPGSGSSTT QGQDVTLAPA TEPASGSAAT WGQDVTSVPV TRPALGSTTP PAHDVTSAPD 130 140 150 160 170 180 NKPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 190 200 210 220 230 240 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 250 260 270 280 290 300 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 310 320 330 340 350 360 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 370 380 390 400 410 420 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 430 440 450 460 470 480 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 490 500 510 520 530 540 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 550 560 570 580 590 600 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 610 620 630 640 650 660 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 670 680 690 700 710 720 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 730 740 750 760 770 780 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 790 800 810 820 830 840 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 850 860 870 880 890 900 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD 910 920 930 940 950 960 TRPAPGSTAP PAHGVTSAPD TRPAPGSTAP PAHGVTSAPD NRPALGSTAP PVHNVTSASG 970 980 990 1000 1010 1020 SASGSASTLV HNGTSARATT TPASKSTPFS IPSHHSDTPT TLASHSTKTD ASSTHHSSVP 1030 1040 1050 1060 1070 1080 PLTSSNHSTS PQLSTGVSFF FLSFHISNLQ FNSSLEDPST DYYQELQRDI SEMFLQIYKQ 1090 1100 1110 1120 1130 1140 GGFLGLSNIK FRPGSVVVQL TLAFREGTIN VHDVETQFNQ YKTEAASRYN LTISDVSVSD 1150 1160 1170 1180 1190 1200 VPFPFSAQSG AGVPGWGIAL LVLVCVLVAL AIVYLIALAV CQCRRKNYGQ LDIFPARDTY 1210 1220 1230 1240 1250 HPMSEYPTYH THGRYVPPSS TDRSPYEKVS AGNGGSSLSY TNPAVAATSA NL
	Isoform 4 (D) [UniParc]. Checksum: B2C6288C94AABC14	FASTA	1,243	121,021
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTG GEKETSATQR SSVPSSTEKN AVSMTSSVLS SHSPGSGSST 70 80 90 100 110 120 TQGQDVTLAP ATEPASGSAA TWGQDVTSVP VTRPALGSTT PPAHDVTSAP DNKPAPGSTA 130 140 150 160 170 180 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 190 200 210 220 230 240 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 250 260 270 280 290 300 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 310 320 330 340 350 360 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 370 380 390 400 410 420 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 430 440 450 460 470 480 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 490 500 510 520 530 540 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 550 560 570 580 590 600 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 610 620 630 640 650 660 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 670 680 690 700 710 720 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 730 740 750 760 770 780 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 790 800 810 820 830 840 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 850 860 870 880 890 900 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DTRPAPGSTA 910 920 930 940 950 960 PPAHGVTSAP DTRPAPGSTA PPAHGVTSAP DNRPALGSTA PPVHNVTSAS GSASGSASTL 970 980 990 1000 1010 1020 VHNGTSARAT TTPASKSTPF SIPSHHSDTP TTLASHSTKT DASSTHHSSV PPLTSSNHST 1030 1040 1050 1060 1070 1080 SPQLSTGVSF FFLSFHISNL QFNSSLEDPS TDYYQELQRD ISEMFLQIYK QGGFLGLSNI 1090 1100 1110 1120 1130 1140 KFRPGSVVVQ LTLAFREGTI NVHDVETQFN QYKTEAASRY NLTISDVSVS DVPFPFSAQS 1150 1160 1170 1180 1190 1200 GAGVPGWGIA LLVLVCVLVA LAIVYLIALA VCQCRRKNYG QLDIFPARDT YHPMSEYPTY 1210 1220 1230 1240 HTHGRYVPPS STDRSPYEKV SAGNGGSSLS YTNPAVAATS ANL
	Isoform 5 (SEC) [UniParc]. Checksum: 6039CBB69974EA3E	FASTA	1,087	103,836
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNAVSMTSSV 70 80 90 100 110 120 LSSHSPGSGS STTQGQDVTL APATEPASGS AATWGQDVTS VPVTRPALGS TTPPAHDVTS 130 140 150 160 170 180 APDNKPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 190 200 210 220 230 240 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 250 260 270 280 290 300 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 310 320 330 340 350 360 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 370 380 390 400 410 420 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 430 440 450 460 470 480 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 490 500 510 520 530 540 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 550 560 570 580 590 600 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 610 620 630 640 650 660 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 670 680 690 700 710 720 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 730 740 750 760 770 780 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 790 800 810 820 830 840 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 850 860 870 880 890 900 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS 910 920 930 940 950 960 APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDNRPALGS TAPPVHNVTS 970 980 990 1000 1010 1020 ASGSASGSAS TLVHNGTSAR ATTTPASKST PFSIPSHHSD TPTTLASHST KTDASSTHHS 1030 1040 1050 1060 1070 1080 SVPPLTSSNH STSPQLSTGV SFFFLSFHIS NLQFNSSLED PSTDYYQELQ RDISEMVSIG LSFPMLP
	Isoform 6 (X) [UniParc]. Checksum: 53B036250EC1242D	FASTA	230	24,566
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNAIPAPTTT 70 80 90 100 110 120 KSCRETFLKW PGSVVVQLTL AFREGTINVH DVETQFNQYK TEAASRYNLT ISDVSVSDVP 130 140 150 160 170 180 FPFSAQSGAG VPGWGIALLV LVCVLVALAI VYLIALAVCQ CRRKNYGQLD IFPARDTYHP 190 200 210 220 230 MSEYPTYHTH GRYVPPSSTD RSPYEKVSAG NGGSSLSYTN PAVAATSANL
	Isoform 7 (Y) [UniParc]. Checksum: 46DC2580CF357BEF	FASTA	255	27,566
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNAFNSSLED 70 80 90 100 110 120 PSTDYYQELQ RDISEMFLQI YKQGGFLGLS NIKFRPGSVV VQLTLAFREG TINVHDVETQ 130 140 150 160 170 180 FNQYKTEAAS RYNLTISDVS VSDVPFPFSA QSGAGVPGWG IALLVLVCVL VALAIVYLIA 190 200 210 220 230 240 LAVCQCRRKN YGQLDIFPAR DTYHPMSEYP TYHTHGRYVP PSSTDRSPYE KVSAGNGGSS 250 LSYTNPAVAA TSANL
	Isoform 8 (Z) [UniParc]. Checksum: B72F7F4FC2D23BCC	FASTA	273	29,592
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNALSTGVSF 70 80 90 100 110 120 FFLSFHISNL QFNSSLEDPS TDYYQELQRD ISEMFLQIYK QGGFLGLSNI KFRPGSVVVQ 130 140 150 160 170 180 LTLAFREGTI NVHDVETQFN QYKTEAASRY NLTISDVSVS DVPFPFSAQS GAGVPGWGIA 190 200 210 220 230 240 LLVLVCVLVA LAIVYLIALA VCQCRRKNYG QLDIFPARDT YHPMSEYPTY HTHGRYVPPS 250 260 270 STDRSPYEKV SAGNGGSSLS YTNPAVAATS ANL
	Isoform 9 (S) [UniParc]. Checksum: 53C6544C2B077B89	FASTA	168	18,277
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNALSTGVSF 70 80 90 100 110 120 FFLSFHISNL QFNSSLEDPS TDYYQELQRD ISEMAVCQCR RKNYGQLDIF PARDTYHPMS 130 140 150 160 EYPTYHTHGR YVPPSSTDRS PYEKVSAGNG GSSLSYTNPA VAATSANL
	Isoform 10 (F) [UniParc]. Checksum: CC2BE70F8C1B325E	FASTA	203	21,556
	10 20 30 40 50 60 MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNAIPAPTTT 70 80 90 100 110 120 KSCRETFLKC FCRFINKGVF WASPILSSVS DVPFPFSAQS GAGVPGWGIA LLVLVCVLVA 130 140 150 160 170 180 LAIVYLIALA VCQCRRKNYG QLDIFPARDT YHPMSEYPTY HTHGRYVPPS STDRSPYEKV 190 200 SAGNGGSSLS YTNPAVAATS ANL

References

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[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: 2394722] [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: 2318825] [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: 1697589] [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: 2268309] [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: 2351132] [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: 2112460] [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: 1688329] [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: 7925397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
[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: 9212228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 7 AND 8), TISSUE SPECIFICITY.
[10]	"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.
[11]	"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: 15969018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), VARIANT MET-1117. Tissue: Cervix carcinoma.
[12]	"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 10).
[13]	NIEHS SNPs program Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-1117 AND ASN-1142.
[14]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]	"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: 3417635] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[16]	"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: 2597151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-160 (ISOFORM 2).
[17]	"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: 8608966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-109 (ISOFORM 2). Tissue: Thyroid.
[18]	"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: 8604237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-89. Tissue: Lung.
[19]	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.
[20]	"Identification of MUC1 proteolytic cleavage sites in vivo." Parry S., Silverman H.S., McDermott K., Willis A., Hollingsworth M.A., Harris A. Biochem. Biophys. Res. Commun. 283:715-720(2001) [PubMed: 11341784] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-33; 28-37 AND 1098-1107, PROTEOLYTIC PROCESSING.
[21]	"The MUC1 SEA module is a self-cleaving domain." Levitin F., Stern O., Weiss M., Gil-Henn C., Ziv R., Prokocimer Z., Smorodinsky N.I., Rubinstein D.B., Wreschner D.H. J. Biol. Chem. 280:33374-33386(2005) [PubMed: 15987679] [Abstract] Cited for: PROTEIN SEQUENCE OF 1098-1111, PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF SER-1098.
[22]	"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: 10373415] [Abstract] Cited for: PROTEIN SEQUENCE OF TANDEM REPEAT, MASS SPECTROMETRY, GLYCOSYLATION.
[23]	"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: 7988707] [Abstract] Cited for: PHOSPHORYLATION.
[24]	"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: 7664271] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SOS1 AND GRB2, INTERACTION WITH GRB2 AND SOS1, PHOSPHORYLATION.
[25]	"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: 7744025] [Abstract] Cited for: GLYCOSYLATION AT THR-131 AND THR-139, MASS SPECTROMETRY.
[26]	"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: 9139698] [Abstract] Cited for: INTERACTION WITH CTNNB1 AND JUP, FUNCTION.
[27]	"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: 9312074] [Abstract] Cited for: GLYCOSYLATION WITHIN TANDEM REPEAT.
[28]	"Developmental expression of mucin genes in the human gastrointestinal system." Reid C.J., Harris A. Gut 42:220-226(1998) [PubMed: 9536947] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[29]	"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: 9597769] [Abstract] Cited for: GLYCOSYLATION AT THR-131 AND THR-139, MASS SPECTROMETRY.
[30]	"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: 9819408] [Abstract] Cited for: INTERACTION WITH GSK3B AND CTNNB1, PHOSPHORYLATION AT SER-1227, MUTAGENESIS OF SER-1223 AND SER-1227.
[31]	"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: 10197628] [Abstract] Cited for: CHARACTERIZATION (ISOFORM Y), MUTAGENESIS OF ASP-1116.
[32]	"MUC1 mucin core protein binds to the domain 1 of ICAM-1." Hayashi T., Takahashi T., Motoya S., Ishida T., Itoh F., Adachi M., Hinoda Y., Imai K. Digestion 63 Suppl. 1:87-92(2001) [PubMed: 11173916] [Abstract] Cited for: INTERACTION WITH ICAM1.
[33]	"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: 11118479] [Abstract] Cited for: SUBCELLULAR LOCATION.
[34]	"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: 11152665] [Abstract] Cited for: INTERACTION WITH SRC; GSK3B AND CTNNB1, PHOSPHORYLATION AT TYR-1229, MUTAGENESIS OF TYR-1229.
[35]	"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: 11350974] [Abstract] Cited for: POLYMORPHISM WITHIN THE REPEAT.
[36]	"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: 11483589] [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.
[37]	"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: 11877440] [Abstract] Cited for: PHOSPHORYLATION AT THR-1224, INTERACTION WITH PRKCD, FUNCTION, MUTAGENESIS OF SER-1223; THR-1224 AND SER-1227.
[38]	"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: 14521915] [Abstract] Cited for: PHOSPHORYLATION AT TYR-1203; TYR-1212; TYR-1229 AND TYR-1243.
[39]	"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: 12750561] [Abstract] Cited for: INTERACTION WITH LYN, PHOSPHORYLATION.
[40]	"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: 14688481] [Abstract] Cited for: INTERACTION WITH CTNNB1, FUNCTION, MUTAGENESIS OF TYR-1229.
[41]	"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: 12441351] [Abstract] Cited for: INTERACTION WITH ADAM17, CLEAVAGE.
[42]	"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: 12832415] [Abstract] Cited for: INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION.
[43]	"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: 12939402] [Abstract] Cited for: INTERACTION WITH ERBB2; ERBB3 AND ERBB4, SUBCELLULAR LOCATION, MUTAGENESIS OF 1187-ARG--LYS-1189.
[44]	"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: 15471854] [Abstract] Cited for: INTERACTION WITH AP1S2 AND GRB2, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-1191; TYR-1203; TYR-1229 AND TYR-1243.
[45]	"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: 15710329] [Abstract] Cited for: INTERACTION WITH TP53, FUNCTION.
[46]	"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: 16288032] [Abstract] Cited for: INTERACTION WITH GSK3B, PHOSPHORYLATION, FUNCTION.
[47]	Erratum Kinlough C.L., Poland P.A., Bruns J.B., Harkleroad K.L., Hughey R.P. J. Biol. Chem. 280:28827-28827(2005)
[48]	"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: 15972891] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[49]	"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: 15513966] [Abstract] Cited for: INTERACTION WITH LCK, PHOSPHORYLATION, FUNCTION, TISSUE SPECIFICITY.
[50]	"Recycling of MUC1 is dependent on its palmitoylation." Kinlough C.L., McMahan R.J., Poland P.A., Bruns J.B., Harkleroad K.L., Stremple R.J., Kashlan O.B., Weixel K.M., Weisz O.A., Hughey R.P. J. Biol. Chem. 281:12112-12122(2006) [PubMed: 16507569] [Abstract] 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.
[51]	"MUC1 oncoprotein stabilizes and activates estrogen receptor alpha." Wei X., Xu H., Kufe D. Mol. Cell 21:295-305(2006) [PubMed: 16427018] [Abstract] Cited for: INTERACTION WITH ESR1.
[52]	"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: 17524503] [Abstract] Cited for: INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, FUNCTION.
[53]	"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: 17308127] [Abstract] Cited for: INTERACTION WITH KLF4, FUNCTION.
[54]	"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: 17545600] [Abstract] Cited for: PHOSPHORYLATION AT TYR-1203; TYR-1218 AND TYR-1229, MUTAGENESIS OF TYR-1203 AND TYR-1218, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[55]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1191; TYR-1203; TYR-1209; TYR-1212; TYR-1218; TYR-1229 AND TYR-1243, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[56]	"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: 16983337] [Abstract] Cited for: INTERACTION WITH EGFR, FUNCTION.
[57]	"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: 16585136] [Abstract] Cited for: STRUCTURE BY NMR OF 1041-1097 AND 1098-1152 OF WILD TYPE AND MUTANT ALA-1098, MASS SPECTROMETRY, STRUCTURE OF CARBOHYDRATES, AUTOCATALYTIC CLEAVAGE.
+	Additional computationally mapped references.

Web resources

Mucin database

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
AF348143 mRNA. Translation: AAK30142.1.
AY327582 mRNA. Translation: AAP97013.1.
AY463543 Genomic DNA. Translation: AAR18816.1.
AL713999 Genomic DNA. Translation: CAI95080.1.
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.

IPI

IPI00013955.
IPI00218163.
IPI00218164.
IPI00218165.
IPI00218166.
IPI00218168.
IPI00218169.
IPI00607673.
IPI00902840.
IPI00978078.

PIR

A35175.

RefSeq

NP_001018016.1. NM_001018016.2.
NP_001018017.1. NM_001018017.2.
NP_001037855.1. NM_001044390.2.
NP_001037856.1. NM_001044391.2.
NP_001037857.1. NM_001044392.2.
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.
NP_001191223.1. NM_001204294.1.
NP_001191224.1. NM_001204295.1.
NP_001191225.1. NM_001204296.1.
NP_001191226.1. NM_001204297.1.
NP_002447.4. NM_002456.5.

UniGene

Hs.89603.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ACM	NMR	-	A	1041-1097	[»]
			B	1098-1152	[»]
2FO4	X-ray	2.70	P	140-146	[»]

ProteinModelPortal

P15941.

SMR

P15941. Positions 1037-1144.

ModBase

Search...

Protein-protein interaction databases

IntAct

P15941. 7 interactions.

MINT

MINT-156679.

STRING

P15941.

Protein family/group databases

MEROPS

S71.001.

PTM databases

GlycoSuiteDB

P15941.

PhosphoSite

P15941.

Polymorphism databases

DMDM

296439295.

Proteomic databases

PRIDE

P15941.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

4582.

KEGG

hsa:4582.

Organism-specific databases

CTD

4582.

GeneCards

GC01M155158.

HGNC

HGNC:7508. MUC1.

HPA

CAB000036.
CAB001986.
HPA004179.
HPA007235.
HPA008855.

MIM

113720. gene.
158340. gene.

neXtProt

NX_P15941.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19101.

Gene expression databases

ArrayExpress

P15941.

Genevestigator

P15941.

GermOnline

ENSG00000185499. Homo sapiens.

Family and domain databases

InterPro

IPR023217. Mucin-1.
IPR000082. SEA.
[Graphical view]

KO

K06568.

PANTHER

PTHR10006. Mucin-1. 1 hit.

Pfam

PF01390. SEA. 1 hit.
[Graphical view]

SMART

SM00200. SEA. 1 hit.
[Graphical view]

PROSITE

PS50024. SEA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

17597.

SOURCE

Search...

Entry information

Entry name

MUC1_HUMAN

Accession

Primary (citable) accession number: P15941
Secondary accession number(s): P13931 , P15942, P17626, Q14128, Q14876, Q16437, Q16442, Q16615, Q7Z552, Q9BXA4, Q9UE75, Q9UE76, Q9UQL1, Q9Y4J2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.