Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01256
Entry Name
UniProt Accession
Theoretical PI
6.96
Molecular Weight
122102.29
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Mucin-1 subunit beta
Protein Synonyms/Alias
MUC-1; Breast carcinoma-associated antigen DF3; Cancer antigen 15-3; CA 15-3; Carcinoma-associated mucin; Episialin; H23AG; Krebs von den Lungen-6; KL-6; PEMT; Peanut-reactive urinary mucin; PUM; Polymorphic epithelial mucin; PEM; Tumor-associated epithelial membrane antigen; EMA; Tumor-associated mucin; CD227; MUC1-NT; MUC1-alpha; MUC1-beta; MUC1-CT;
Gene Name
MUC1
Gene Synonyms/Alias
PUM;
Created Date
01-APR-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
1184
Canonical
YLIALAVCQCRRKNY
[1]
S-Palmitoylation
1186
Canonical
IALAVCQCRRKNYGQ
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Kinlough CL, McMahan RJ, Poland PA, Bruns JB, Harkleroad KL, Stremple RJ,Kashlan OB, Weixel KM, Weisz OA, Hughey RP. Recycling of MUC1 is dependent on itspalmitoylation. J Biol Chem. 2006 Apr 28;281(17):12112-22. Epub 2006 Feb 28.[PMID:16507569]
Functional Description
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.
Sequence Annotation
Topological domain: 24 1158 Extracellular.
Transmembrane: 1159 1181 Helical.
Topological domain: 1182 1255 Cytoplasmic.
Domain: 1039 1148 SEA.
Region: 126 965 42 X 20 AA approximate tandem repeats ofP-A-P-G-S-T-A-P-P-A-H-G-V-T-S-A-P-D-T-R.
Region: 1192 1228 Interaction with P53.
Region: 1223 1230 Required for interaction with GSK3B.
Region: 1233 1241 Required for interaction with beta- andgamma-catenins.
Motif: 1203 1206 Interaction with GRB2.
Motif: 1229 1232 Interaction with SRC and ESR1.
Motif: 1243 1246 Required for interaction with AP1S2.
Functional site: 1097 1098 Cleavage; by autolysis.
Modified residue: 1191 1191 Phosphotyrosine.
Modified residue: 1203 1203 Phosphotyrosine; by PDGFR.
Modified residue: 1209 1209 Phosphotyrosine.
Modified residue: 1212 1212 Phosphotyrosine.
Modified residue: 1218 1218 Phosphotyrosine; by PDGFR.
Modified residue: 1224 1224 Phosphothreonine; by PKC/PRKCD.
Modified residue: 1227 1227 Phosphoserine; by GSK3-beta.
Modified residue: 1229 1229 Phosphotyrosine; by CSK, EGFR and SRC.
Modified residue: 1243 1243 Phosphotyrosine.
Protein Length
1255 AA.
Protein Sequence
(Canonical)
MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNAVSMTSSV  60
LSSHSPGSGS STTQGQDVTL APATEPASGS AATWGQDVTS VPVTRPALGS TTPPAHDVTS  120
APDNKPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  180
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  240
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  300
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  360
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  420
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  480
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  540
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  600
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  660
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  720
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  780
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  840
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS  900
APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDNRPALGS TAPPVHNVTS  960
ASGSASGSAS TLVHNGTSAR ATTTPASKST PFSIPSHHSD TPTTLASHST KTDASSTHHS  1020
SVPPLTSSNH STSPQLSTGV SFFFLSFHIS NLQFNSSLED PSTDYYQELQ RDISEMFLQI  1080
YKQGGFLGLS NIKFRPGSVV VQLTLAFREG TINVHDVETQ FNQYKTEAAS RYNLTISDVS  1140
VSDVPFPFSA QSGAGVPGWG IALLVLVCVL VALAIVYLIA LAVCQCRRKN YGQLDIFPAR  1200
DTYHPMSEYP TYHTHGRYVP PSSTDRSPYE KVSAGNGGSS LSYTNPAVAA TSANL       1255
FASTA
(Canonical)
>LipidDB-9606-01256|P15941
MTPGTQSPFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSV
LSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTS
APDNKPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS
APDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDNRPALGSTAPPVHNVTS
ASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLASHSTKTDASSTHHS
SVPPLTSSNHSTSPQLSTGVSFFFLSFHISNLQFNSSLEDPSTDYYQELQRDISEMFLQI
YKQGGFLGLSNIKFRPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVS
VSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPAR
DTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL
Gene Ontology
GO:0016324; C:apical plasma membrane; IBA:RefGenome
GO:0009986; C:cell surface; IBA:RefGenome
GO:0005737; C:cytoplasm; IBA:RefGenome
GO:0005615; C:extracellular space; IDA:UniProt
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005796; C:Golgi lumen; TAS:Reactome
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0000790; C:nuclear chromatin; IDA:BHF-UCL
GO:0031982; C:vesicle; IDA:UniProtKB
GO:0002039; F:p53 binding; IPI:BHF-UCL
GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:BHF-UCL
GO:0003712; F:transcription cofactor activity; IDA:BHF-UCL
GO:0044267; P:cellular protein metabolic process; TAS:Reactome
GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl
GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IDA:BHF-UCL
GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:BHF-UCL
GO:0030855; P:epithelial cell differentiation; IEA:Ensembl
GO:0007565; P:female pregnancy; IEA:Ensembl
GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:BHF-UCL
GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:BHF-UCL
GO:0016266; P:O-glycan processing; TAS:Reactome
GO:0090240; P:positive regulation of histone H4 acetylation; IDA:BHF-UCL
GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IDA:BHF-UCL
GO:0043687; P:post-translational protein modification; TAS:Reactome
GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IDA:BHF-UCL
GO:0001666; P:response to hypoxia; IEA:Ensembl
Interpro
InterPro; IPR023217; Mucin-1
InterPro; IPR000082; SEA_dom
Pfam
Pfam; PF01390; SEA;
SMART
SMART; SM00200; SEA;
PROSITE
PROSITE; PS50024; SEA;
PRINTS