Search by BoMiProt ID - Bomi129


Primary Information

BoMiProt ID Bomi129
Protein Name Ras-related C3 botulinum toxin substrate 1
Organism Bos taurus
Uniprot IDP62998
Milk FractionWhey
Ref Sequence ID NP_776588.1
Aminoacid Length 192
Molecular Weight 21450
FASTA Sequence Download
Gene Name RAC1
Gene ID 281440
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Presence in other biological fluids/tissue/cells Rac1 and Rac3 are ubiquitously expressed and therefore regulate a wide variety of cellular processes, whereas Rac2 is predominantly expressed in cells of the hematopoietic lineage; Rac1b was discovered in human tumors;
Protein Function act as molecular switches cycling between an active GTP‐bound and an inactive GDP‐bound form through nucleotide exchange and hydrolysis; three distinct mammalian Rac isoforms, Rac1, 2 and 3, share a very high sequence identity; Rac2 is proposed to be responsible for the regulation of the oxidative burst in hematopoietic cells; serum‐inducible and hyperactive in breast cancer cells;
Biochemical Properties Rac1b showed an increase in its intrinsic nucleotide dissociation, which cannot be further enhanced by Tiam1; (2) a drastic decrease in intrinsic GTP‐hydrolysis rate, which can be restored by GAP; and (3) reduced affinity for PAK‐GBD. The altered characteristics of Rac1b are based on an open switch I conformation and a highly mobile switch II, which are induced by the 19 amino acid insertion
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions 59-74,177-192
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography 1. Jordan, P., Brazão, R., Boavida, M. G., Gespach, C., & Chastre, E. (1999). Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors. Oncogene, 18(48), 6835–6839. https://doi.org/10.1038/sj.onc.1203233.
2. Haeusler, L. C., Blumenstein, L., Stege, P., Dvorsky, R., & Ahmadian, M. R. (2003). Comparative functional analysis of the Rac GTPases. FEBS Letters, 555(3), 556–560. https://doi.org/10.1016/S0014-5793(03)01351-6.
3. Fiegen, D., Haeusler, L.-C., Blumenstein, L., Herbrand, U., Dvorsky, R., Vetter, I. R., & Ahmadian, M. R. (2004). Alternative splicing of Rac1 generates Rac1b, a self-activating GTPase. The Journal of Biological Chemistry, 279(6), 4743–4749. https://doi.org/10.1074/jbc.M310281200.
4. Haataja, L., Groffen, J., & Heisterkamp, N. (1997). Characterization of RAC3, a novel member of the Rho family. The Journal of Biological Chemistry, 272(33), 20384–20388. https://doi.org/10.1074/jbc.272.33.20384.