Search by BoMiProt ID - Bomi9021


Primary Information

BoMiProt ID Bomi9021
Protein Name Septin-1
Organism Bos taurus
Uniprot IdA5PJU9
Milk FractionWhey
Ref Sequence Id NP_001092417.1
Aminoacid Length 367
Molecular Weight 41983
Fasta Sequence https://www.uniprot.org/uniprot/A5PJU9.fasta
Gene Name SEPTIN1/SEPT1
Gene Id 512478
Protein Existence Status reviewed

Secondary Information

Protein Function Septin 1 is a member of an evolutionarily conserved family of GTP-binding and filament-forming proteins named septins, which function in diverse processes including cytokinasis, vesicle trafficking, apoptosis, remodelling of the cytoskeleton, infection, neurodegeneration and neoplasia.
Biochemical Properties Septins are an evolutionarily conserved group of GTP-binding and filament-forming proteins that belong to the large superclass of P-loop GTPases. The septins were first recognized in Saccharomyces cerevisiae as a set of homologous proteins (the products of the CDC3, CDC10, CDC11 and CDC12 genes) associated with the 10 nm filaments found at the cytoplasmic face of the plasma membrane in the mother-bud neck
PTMs Phosphorylation at Ser/Thr
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|A5PJU9|SEPT1_BOVIN Septin-1 OS=Bos taurus OX=9913 GN=SEPTIN1 PE=2 SV=1 MDKEYVGFAALPNQLHRKSVKKGFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQIPEAS ARLTQTLTIERRGVEIEEGGIKVKLTVVDTPGFGDSVDCSDCWLPVVRFIEEQFEQYLRD ESGLNRKNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPKET QALKQKIREQLKEEEINIYQFPECDS*206DEDEDFKRQDAEMKESIPFAVVGSCEVVRDGGPR PVRGRHYS*248WGT*251VEVENPHHCDFLNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQSLARP GARDRAS*307RSKLSRQS*315ATEIPLPMLPLADTEKLIREKDEELRRMQEMLEKMQAQMQLSQAQ GEQSDAL
Predicted Disorder Regions 202-211, 298-367
DisProt Annotation
TM Helix Prediction no TM helices
Additional Comments Septin 1 with site-directed mutations of five serine residues (Ser19, Ser206, Ser307, Ser312 and Ser315) has a much lower degree of aggregation and better structural homogeneity and that the mutations cause only slight perturbations in the secondary structure of septin 1.
Bibliography 1.Hu H, Yu WB, Li SX, Ding XM, Yu L, Bi RC. Crystallization and preliminary crystallographic studies of human septin 1 with site-directed mutations. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Feb 1;62(Pt 2):128-32. doi: 10.1107/S1744309105043228. Epub 2006 Jan 27. PMID: 16511282; PMCID: PMC2150944.