Search by BoMiProt ID - Bomi5021


Primary Information

BoMiProt ID Bomi5021
Protein Name Damage-control phosphatase ARMT1/Acidic residue methyltransferase 1/Protein-glutamate O-methyltransferase/Sugar phosphate phosphatase ARMT1
Organism Bos taurus
Uniprot IdA3KMX8
Milk FractionWhey
Ref Sequence Id NP_001076968.1
Aminoacid Length 441
Molecular Weight 50964
Fasta Sequence https://www.uniprot.org/uniprot/A3KMX8.fasta
Gene Name ARMT1
Gene Id 540698
Protein Existence Status reviewed

Secondary Information

Protein Function shows phosphatase activity against several substrates andshown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues.
Biochemical Properties The biochemical activities of the human protein are conserved with those of a previously characterized budding yeast homolog, where an in vitro phosphatase activity is supported by divalent cations that include Co2+, Ni2+, Mn2+ or Mg2+.
PTMs Acetylation and phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|A3KMX8|ARMT1_BOVIN Damage-control phosphatase ARMT1 OS=Bos taurus OX=9913 GN=ARMT1 PE=2 SV=1 MAGPPASLSARDVGSFAYLSVKDRSPQILTKAIDTLHRHKSEFFEKHGEKGLEAEKKAIS LLSKLRNELQTDKPIVPLVEKFVDTDIWNQYLEYQQSLLNES*102DGKPRWFLSPWLFVECYM YRRIHEAIIQSPPIDDFDIFKEFKDQNFFESQESIIALCTHLQELRKTIEDLDENQLKNE FFKVLQISLWGNKCDLSLSGGEHISQKTNIMNSLEDLKPFILVNDMDRLWSLLSNCKKTR EKESVTRVDIVLDNSGFELITDLVLADFLLSSKLATKIHFYGKTIPWFVSDTTLHDFNWI IKQLKHSNNKWVSQCGVDWEDHVKTGRWVYLDHIFWTLPHEFSAMSQVAPDLHAALQKAH LIFFKGDLNYRKLTGDRRWEFTVPFHEALSGFHPAPLCSIRTLKAEVQVGLQPGQGEQLT ASEPNWLTAGKYGVFQFDGPL
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments The sequence around the two cysteines involved in the redox-active disulphide bond is conserved and can be used as a signature pattern.
Bibliography 1.Dennis TN, Kenjić N, Kang AS, Lowenson JD, Kirkwood JS, Clarke SG, Perry JJP. Human ARMT1 structure and substrate specificity indicates that it is a DUF89 family damage-control phosphatase. J Struct Biol. 2020 Oct 1;212(1):107576. doi: 10.1016/j.jsb.2020.107576. Epub 2020 Jul 15. PMID: 32682077.