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Protein arginine methyltransferase 5 information


PRMT5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPRMT5, HRMT1L5, IBP72, JBP1, SKB1, SKB1Hs, Protein arginine methyltransferase 5, HSL7
External IDsOMIM: 604045; MGI: 1351645; HomoloGene: 4454; GeneCards: PRMT5; OMA:PRMT5 - orthologs
EC number2.1.1.321
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_013768
NM_001313906
NM_001313907

RefSeq (protein)

NP_001300835
NP_001300836
NP_038796

Location (UCSC)Chr 14: 22.92 – 22.93 MbChr 14: 54.74 – 54.75 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein arginine N-methyltransferase 5 is an enzyme that in humans is encoded by the PRMT5 gene.[5][6] PRMT5 symmetrically dimethylates H2AR3, H4R3, H3R2, and H3R8 in vivo, all of which are linked to a range of transcriptional regulatory events.[7]

PRMT5 is a highly conserved arginine methyltransferase that translocated from the cytoplasm to the nucleus at embryonic day ~E8.5, and during preimplantation development at the ~4-cell stage.[8]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100462 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023110 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Gilbreth M, Yang P, Bartholomeusz G, et al. (Jan 1999). "Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs". Proc Natl Acad Sci U S A. 95 (25): 14781–6. doi:10.1073/pnas.95.25.14781. PMC 24526. PMID 9843966.
  6. ^ "Entrez Gene: PRMT5 protein arginine methyltransferase 5".
  7. ^ Stopa N, Krebs JE, Shechter D (June 2015). "The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond". Cellular and Molecular Life Sciences. 72 (11): 2041–59. doi:10.1007/s00018-015-1847-9. PMC 4430368. PMID 25662273.
  8. ^ Kim S, Gunesdogan, U, et al. (Nov 2014). "PRMT5 Protects Genomic Integrity during Global DNA Demethylation in Primordial Germ Cells and Preimplantation Embryos". Molecular Cell. 56 (4): 564–579. doi:10.1016/j.molcel.2014.10.003. PMC 4250265. PMID 25457166.

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Protein arginine methyltransferase 5

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Protein arginine N-methyltransferase 5 is an enzyme that in humans is encoded by the PRMT5 gene. PRMT5 symmetrically dimethylates H2AR3, H4R3, H3R2, and...

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Methyltransferase

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include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM dependent methyltransferases. SAM is the...

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Histone methyltransferase

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Histone methyltransferases (HMT) are histone-modifying enzymes (e.g., histone-lysine N-methyltransferases and histone-arginine N-methyltransferases), that...

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Protein methylation

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side-chains of arginine and lysine, but also at the amino- and carboxy-termini of a number of different proteins. In biology, methyltransferases catalyze the...

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Arginine

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Another post-translational modification of arginine involves methylation by protein methyltransferases. Arginine is the immediate precursor of nitric oxide...

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IWS1

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interacts with protein arginine methyltransferase 5 (PRMT5), is essential for cell survival. It also recruits a SET2 histone methyltransferase (Huntingtin-interacting...

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Methylation

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dimethylarginine), by protein arginine methyltransferases (PRMTs). Lysine can be methylated once, twice, or three times by lysine methyltransferases. Protein methylation...

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PRMT2

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Protein arginine N-methyltransferase 2 is an enzyme that in humans is encoded by the PRMT2 gene. The enzyme methylates final nitrogen atom of arginine...

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Essential amino acid

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the infant or individuals in severe catabolic distress. These six are arginine, cysteine, glycine, glutamine, proline, and tyrosine. Six amino acids are...

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Protein biosynthesis

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the amino acids lysine and arginine. One example of a protein which is commonly methylated is a histone. Histones are proteins found in the nucleus of the...

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SUPT5H

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Cyclin-dependent kinase 7, HTATSF1, PIN1, POLR2A, PRMT1 and Protein arginine methyltransferase 5. GRCh38: Ensembl release 89: ENSG00000196235 – Ensembl, May...

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Protein detoxification

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Protein detoxification is the process by which proteins containing methylated arginine are broken down and removed from the body. Arginine (Arg) is a non-essential...

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PRMT1

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Protein arginine N-methyltransferase 1 is an enzyme that in humans is encoded by the PRMT1 gene. The HRMT1L2 gene encodes a protein arginine methyltransferase...

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Histone methylation

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histone 3 (H3K4me1), and arginine (R) residues on H3 and H4. Addition of methyl groups to histones by histone methyltransferases, can either activate or...

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Tudor domain

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activation depending on the Tudor domain protein and context. For example, the human TDRD3 protein binds methylated arginine residues and promotes transcription...

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RIOK1

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Grimmler M (January 2011). "RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5...

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Methionine

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the enzyme betaine-homocysteine methyltransferase (E.C.2.1.1.5, BHMT). BHMT makes up to 1.5% of all the soluble protein of the liver, and recent evidence...

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Histone

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In biology, histones are highly basic proteins abundant in lysine and arginine residues that are found in eukaryotic cell nuclei and in most Archaeal phyla...

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PRMT6

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Protein arginine N-methyltransferase 6 is an enzyme that in humans is encoded by the PRMT6 gene. Protein arginine N-methyltransferases, such as PRMT6,...

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NDUFAF7

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Protein arginine methyltransferase NDUFAF7, mitochondrial, also known as NADH:ubiquinone oxidoreductase complex assembly factor 7 (NDUFAF7), MidA, C2orf56...

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Fibrillarin

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increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1". Journal of...

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SnRNP

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arginine methyltransferase-5 (PRMT5) protein. SmD3, SmB and SmD1 undergo post-translational modification in the methylosome. These three Sm proteins have...

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Ras GTPase

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C-terminus by a specific prenyl-protein specific endoprotease and the new C-terminus is methylated by a methyltransferase. KRas processing is completed...

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