Search by BoMiProt ID - Bomi7840


Primary Information

BoMiProt ID Bomi7840
Protein Name Paternally-expressed gene 3 protein
Organism Bos taurus
Uniprot IDQ6H236
Milk FractionWhey
Aminoacid Length 2387
Molecular Weight 264828
FASTA Sequence Download
Gene Name PEG3
Protein Existence Status reviewed

Secondary Information

Protein Function The structure of SCAN domain from PEG3, a predicted transcription factor,serves to identify key residues important to the creation of the PEG3- SCAN dimer interface.
Biochemical Properties The protein carries twelve zinc finger DNAbinding motifs, which are an important component of transcription. These zinc fingers are classed as Cys2-His2 Kru¨ppel-type motifs where metal ion coordination helps to stabilize a simple bba fold
PTMs Omega-N-methylation at rginine,Phosphorylation at Ser/Thr
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 Phosphorylation by casein kinase II upon estrogen stimulation, induces the release by KANK2 of NCOA1 and its translocation to the nucleus where NCOA1 can activate gene transcription
Bibliography 1.Rimsa V, Eadsforth TC, Hunter WN. Structure of the SCAN domain of human paternally expressed gene 3 protein. PLoS One. 2013 Jul 23;8(7):e69538. doi: 10.1371/journal.pone.0069538. PMID: 23936039; PMCID: PMC3720700. 2.Relaix F, Weng X, Marazzi G, Yang E, Copeland N, et al. (1996) Pw1, a novel zinc finger gene implicated in the myogenic and neuronal lineages. Dev Biol 177: 383–396. 3.. Miller J, McLachlan AD, Klug A (1985) Repetitive zinc-binding domains in the protein transcription factor III A from Xenopus oocytes. EMBO J 4: 1609–1614. 4. Berg JM (1988) Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins. Proc Natl Acad Sci U S A 85: 99–102. 5. Lee MS, Gippert GP, Soman KV, Case DA, Wright PE (1989) Threedimensional solution structure of a single zinc finger DNA-binding domain. Science 245: 635–637.