Search by BoMiProt ID - Bomi3848


Primary Information

BoMiProt ID Bomi3848
Protein Name ALS2 C-terminal-like protein
Organism Bos taurus
Uniprot IdA6QP75
Milk FractionWhey
Ref Sequence Id NP_001095958.1
Aminoacid Length 953
Molecular Weight 107869
Fasta Sequence https://www.uniprot.org/uniprot/A6QP75.fasta
Gene Name ALS2CL
Gene Id 506969
Protein Existence Status reviewed

Secondary Information

Protein Function  Acts as a guanine nucleotide exchange factor (GEF) for Rab5 GTPase. Regulates the ALS2-mediated endosome dynamics.ALS2CL is a novel factor modulating the Rab5-mediated endosome dynamics in the cells.
Biochemical Properties Analysis of the predicted amino acid sequences revealed a high level of sequence similarity throughout the entire region of ALS2CL and the C-terminal portion of the ALS2 proteins, indicating that ALS2CL/Als2cl and ALS2/Als2 were evolutionally conserved genes evolved from a common ancestry of origin.
PTMs N6-acetylation of Lys-44, Phosphorylation at many AA residues, Ubl conjugation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
na
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction no TM helices
Significance of PTMs Autophosphorylation at Thr-186, Ser-347, Thr-350, Ser-353, Thr-354 and Ser-357 triggers kinase activity by promoting cyclin and substrate binding upon conformational changes.Phosphorylation at Thr-186 requires the calcium Ca2+ signaling pathway, including CaMK1D and calmodulin.N6-acetylation of Lys-44 promotes kinase activity, whereas acetylation of both Lys-44 and Lys-48 mediated by PCAF/KAT2B and GCN5/KAT2A reduces kinase activity.
Additional Comments ALS2 may implicate in the vesicle/membrane dynamics in the cells through the activation of Rab5.
Bibliography Hadano S, Otomo A, Suzuki-Utsunomiya K, Kunita R, Yanagisawa Y, Showguchi-Miyata J, Mizumura H, Ikeda JE. ALS2CL, the novel protein highly homologous to the carboxy-terminal half of ALS2, binds to Rab5 and modulates endosome dynamics. FEBS Lett. 2004 Sep 24;575(1-3):64-70. doi: 10.1016/j.febslet.2004.07.092. PMID: 15388334.