Search by BoMiProt ID - Bomi598

Primary Information

BoMiProt ID Bomi598
Protein Name AP-2 complex subunit mu
Organism Bos taurus
Uniprot IDQ3ZC13
Milk FractionExosome
Ref Sequence ID NP_001029695.1
Aminoacid Length 435
Molecular Weight 49655
FASTA Sequence Download
Gene Name AP2M1
Gene ID 517446
Protein Existence Status Reveiwed:Experimental evidence at transcript level

Secondary Information

Protein Function AP-2 facilitates clathrin-mediated endocytosis of a wide range of proteins including receptors, adhesion molecules and viral proteins; mediate intracellular membrane trafficking along endocytic and secretory transport pathways; AP complexes localize to different intracellular compartments and mediate membrane trafficking in distinct pathways; recognize and concentrate cargo proteins into vesicular carriers that mediate transport from a donor membrane to a target organellar membrane; play important roles in maintaining the normal physiological function of eukaryotic cells
Biochemical Properties heterotetrameric protein complexes; five different AP complexes: AP-1, AP-2 and AP-3 are clathrin-associated complexes; whereas AP-4 and AP-5 are not; selective recruitment of AP-2 to plasma membrane occurs by binding of the α and μ2 subunits to PIP2; ADP-ribosylation factor) 6 may also contribute to the membrane recruitment of AP-2;
Linking IDs Bomi43
Bibliography 1. Nolen, B. J., Littlefield, R. S., & Pollard, T. D. (2004). Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP. Proceedings of the National Academy of Sciences of the United States of America, 101(44), 15627–15632.
2. Jackson, L. P., Kelly, B. T., McCoy, A. J., Gaffry, T., James, L. C., Collins, B. M., … Owen, D. J. (2010). A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. Cell, 141(7), 1220–1229.
3. Rappoport, J. Z., & Simon, S. M. (2009). Endocytic trafficking of activated EGFR is AP-2 dependent and occurs through preformed clathrin spots. Journal of Cell Science, 122(Pt 9), 1301–1305.
4. Holloway, Z. G., Velayos-Baeza, A., Howell, G. J., Levecque, C., Ponnambalam, S., Sztul, E., & Monaco, A. P. (2013). Trafficking of the Menkes copper transporter ATP7A is regulated by clathrin-, AP-2-, AP-1-, and Rab22-dependent steps. Molecular Biology of the Cell, 24(11), 1735–1748, S1-8.
5. Kastning, K., Kukhtina, V., Kittler, J. T., Chen, G., Pechstein, A., Enders, S., … Haucke, V. (2007). Molecular determinants for the interaction between AMPA receptors and the clathrin adaptor complex AP-2. Proceedings of the National Academy of Sciences of the United States of America, 104(8), 2991–2996.
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions
DisProt Annotation
TM Helix Prediction No TM helices
PDB ID 6QH6, 6QH7,