Search by BoMiProt ID - Bomi8364


Primary Information

BoMiProt ID Bomi8364
Protein Name Protein LSM14 homolog A/Protein FAM61A/RNA-associated protein 55A
Organism Bos taurus
Uniprot IdQ3MHF8
Milk FractionWhey
Ref Sequence Id NP_001029826.1
Aminoacid Length 463
Molecular Weight 50636
Fasta Sequence https://www.uniprot.org/uniprot/Q3MHF8.fasta
Gene Name LSM14A/RAP55A
Gene Id 538838
Protein Existence Status reviewed

Secondary Information

Protein Function Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for translationally inactive mRNAs and protect them from degradation.Acts as a repressor of mRNA translation
Biochemical Properties The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing.The N-terminal LSM domain of LSM14 is a common fold among decapping factors and is also found in the LSM1-7 proteins and EDC3. However, in contrast to LSM1-7 proteins, whose LSM domains interact to form a heteroheptameric ring-like structure with RNA-binding properties, the LSM domains in LSM14 and EDC3 diverge functionally and serve as interaction platforms for other protein factors
PTMs Acetylation,Methylation and Phosphorylation at Ser and Thr
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q3MHF8|LS14A_BOVIN Protein LSM14 homolog A OS=Bos taurus OX=9913 GN=LSM14A PE=2 SV=1 MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDE VFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSTSSFQSVGSYGPFGRMPTY SQFSPSSLVGQQFGAVGVAGSSLTSFGTEASSSSALSQSSVVGSAFTQDSRALKTQLS*178QG RS*182S*183PQLDPLRKS*192PT*194MEQAVQTASAHLPAPAPVGRRS*216PVSTRPLPSTS*227QKPIENQEHRRAEVHKVSRPENEQLRNDSKRQIVPGAPSAPRRGRGGHRGGRGRFGIRRDGPMKFEKDFDFES ANAQFNKEEIDREFHNKLKLKEDKLEKQEKPVNGEDKGDSGVDTQNSEGNADEEDPLGPN CYYDKTKSFFDNISCDDNRERRPTWAEERRLNAETFGIPLR*401PNRGRGGYRGRGGLGFRGG RGRGSGRGGAFTTPRGFRGGFRGGRGGREFADFEYRKDNKVAA
Predicted Disorder Regions 172-288, 322-359, 398-448
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs SCD6 efficiently interacts with eIF4G1 in a manner dependent on Hmt1-mediated methylation of the SCD6 RGG motif, and that this is required to induce translational repression.
Bibliography 1.Yang WH, Yu JH, Gulick T, Bloch KD, Bloch DB. RNA-associated protein 55 (RAP55) localizes to mRNA processing bodies and stress granules. RNA. 2006 Apr;12(4):547-54. doi: 10.1261/rna.2302706. Epub 2006 Feb 16. PMID: 16484376; PMCID: PMC1421083. 2.Brandmann T, Fakim H, Padamsi Z, Youn JY, Gingras AC, Fabian MR, Jinek M. Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes. EMBO J. 2018 Apr 3;37(7):e97869. doi: 10.15252/embj.201797869. Epub 2018 Mar 6. PMID: 29510985; PMCID: PMC5881628. 3.Poornima G, Shah S, Vignesh V, Parker R, Rajyaguru PI (2016) Arginine methylation promotes translation repression activity of eIF4G-binding protein, Scd6. Nucleic Acids Res 44: 9358–9368