Search by BoMiProt ID - Bomi192


Primary Information

BoMiProt ID Bomi192
Protein Name TAP1 protein
Organism Bos taurus
Uniprot IDA6QPZ6
Milk FractionMFGM
Ref Sequence ID XP_005223309.1
Aminoacid Length 750
Molecular Weight 81950
FASTA Sequence Download
Gene Name TAP1
Gene ID 524959
Protein Existence Status Unreviewed: Experimental evidence at transcript level

Secondary Information

Protein Function ER-resident chaperone molecules; transporter associated with antigen processing (TAP) is essential for the transport of antigenic peptides across the membrane of the endoplasmic reticulum; peptides are transported from the cytosol into the lumen of the endoplasmic reticulum (ER) by a peptide transporter, which is known as the transporter associated with antigen processing; tapasin facilitates the binding of high affinity peptides; TAP-1 and TAP-2, tapasin, calnexin, calreticulin, and ERp57 together assist in the formation of H chain/ 2m/peptide trimers that, once stably assembled, transit to the cell surface
Biochemical Properties TAP interacts with major histocompatibility complex class I heavy chain (HC)Ɣß2-microglobulin (ß2-m) dimers; TAP consists of two subunits, TAP1 and TAP2, both members of the ATP-binding cassette transporters
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Bibliography 1. Vigneron, N., Peaper, D. R., Leonhardt, R. M., & Cresswell, P. (2009). Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentation. European Journal of Immunology, 39(9), 2371–2376. https://doi.org/10.1002/eji.200939536.
2. Carreno, B. M., Solheim, J. C., Harris, M., Stroynowski, I., Connolly, J. M., & Hansen, T. H. (1995). TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. Journal of Immunology (Baltimore, Md. : 1950), 155(10), 4726–4733. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/7594473.
3. Li, S., Sjögren, H. O., Hellman, U., Pettersson, R. F., & Wang, P. (1997). Cloning and functional characterization of a subunit of the transporter associated with antigen processing. Proceedings of the National Academy of Sciences of the United States of America, 94(16), 8708–8713. https://doi.org/10.1073/pnas.94.16.8708.
4. Lybarger, L., Yu, Y. Y., Chun, T., Wang, C. R., Grandea, A. G., Van Kaer, L., & Hansen, T. H. (2001). Tapasin enhances peptide-induced expression of H2-M3 molecules, but is not required for the retention of open conformers. Journal of Immunology (Baltimore, Md. : 1950), 167(4), 2097–2105. https://doi.org/10.4049/jimmunol.167.4.2097.
5. Williams, A. P., Peh, C. A., Purcell, A. W., McCluskey, J., & Elliott, T. (2002). Optimization of the MHC class I peptide cargo is dependent on tapasin. Immunity, 16(4), 509–520. https://doi.org/10.1016/s1074-7613(02)00304-7.