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Protein Page:
MUC17 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
MUC17 Probably plays a role in maintaining homeostasis on mucosal surfaces. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Membrane protein, integral; Cell adhesion
Cellular Component: Golgi lumen; apical plasma membrane; extracellular region; integral to membrane; external side of plasma membrane
Molecular Function: protein binding; extracellular matrix constituent, lubricant activity; PDZ domain binding
Biological Process: cellular protein metabolic process; O-glycan processing; cellular homeostasis; post-translational protein modification
Reference #:  Q685J3 (UniProtKB)
Alt. Names/Synonyms: membrane mucin MUC17; MUC-17; MUC-3; MUC17; MUC3; mucin 17, cell surface associated; Mucin-17; secreted mucin MUC17; small intestinal mucin MUC3; Small intestinal mucin-3
Gene Symbols: MUC17
Molecular weight: 451,741 Da
Basal Isoelectric point: 4.03  Predict pI for various phosphorylation states
Select Structure to View Below

MUC17

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S56-ga NRQCQQLsQHVRTGS
  mouse

 
- gap
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