Protein arginine methyltransferase 5: Difference between revisions

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{{Infobox_gene}}
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'''Protein arginine N-methyltransferase 5''' is an [[enzyme]] that in humans is encoded by the ''PRMT5'' [[gene]].<ref name="pmid9843966">{{cite journal | vauthors = Gilbreth M, Yang P, Bartholomeusz G, Pimental RA, Kansra S, Gadiraju R, Marcus S | title = Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs | journal = Proc Natl Acad Sci U S A | volume = 95 | issue = 25 | pages = 14781–6 | date = Jan 1999 | pmid = 9843966 | pmc = 24526 | doi = 10.1073/pnas.95.25.14781 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRMT5 protein arginine methyltransferase 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10419| accessdate = }}</ref>  PRMT5 symmetrically dimethylates H2AR3, H4R3, H3R2, and H3R8 in vivo, all of which are linked to a range of transcriptional regulatory events (Cell. Mol. Life Sci. (2015) 72:2041–2059 DOI 10.1007/s00018-015-1847-9)
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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.<ref>{{cite journal | vauthors = Kim S, Gunesdogan, U, Zylicz JJ, Hackett, JA, Cougot, D, Bao, S, Lee, C, Dietmann, S, Allen, GE, Sngupta, R, Surani MA | title = PRMT5 Protects Genomic Integrity during Global DNA Demethylation in Primordial Germ Cells and Preimplantation Embryos | journal = Molecular Cell | volume = 56 | pages = 564–579 | date = Nov 2014 | doi = 10.1016/j.molcel.2014.10.003 }}</ref>
{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = Protein arginine methyltransferase 5
| HGNCid = 10894
| Symbol = PRMT5
| AltSymbols =; HRMT1L5; IBP72; JBP1; SKB1; SKB1Hs
| OMIM = 604045
| ECnumber = 
| Homologene = 4454
| MGIid = 1351645
| GeneAtlas_image1 = PBB_GE_PRMT5_217786_at_tn.png
| Function = {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0008469 |text = histone-arginine N-methyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007088 |text = regulation of mitosis}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0016568 |text = chromatin modification}} {{GNF_GO|id=GO:0035246 |text = peptidyl-arginine N-methylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10419
    | Hs_Ensembl = ENSG00000100462
    | Hs_RefseqProtein = NP_001034708
    | Hs_RefseqmRNA = NM_001039619
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 22459579
    | Hs_GenLoc_end = 22468501
    | Hs_Uniprot = O14744
    | Mm_EntrezGene = 27374
    | Mm_Ensembl = ENSMUSG00000023110
    | Mm_RefseqmRNA = NM_013768
    | Mm_RefseqProtein = NP_038796
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 53461387
    | Mm_GenLoc_end = 53471564
    | Mm_Uniprot = Q9CRT9
  }}
}}
'''Protein arginine methyltransferase 5''', also known as '''PRMT5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRMT5 protein arginine methyltransferase 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10419| accessdate = }}</ref>


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==Model organisms==
{{PBB_Summary
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
| section_title =
|+ ''Prmt5'' knockout mouse phenotype
| summary_text =
|-
}}
! Characteristic!! Phenotype


==References==
|-
{{reflist|2}}
| [[Homozygote]] viability || bgcolor="#C40000"|Abnormal
==Further reading==
|-
| [[Recessive]] lethal study || bgcolor="#C40000"|Abnormal
|-
| Fertility || bgcolor="#488ED3"|Normal
|-
| Body weight || bgcolor="#488ED3"|Normal
|-
| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
|-
| Neurological assessment || bgcolor="#488ED3"|Normal
|-
| Grip strength || bgcolor="#488ED3"|Normal
|-
| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
|-
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
|-
| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal
|-
| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
|-
| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
|-
| [[Radiography]] || bgcolor="#488ED3"|Normal
|-
| Body temperature || bgcolor="#488ED3"|Normal
|-
| Eye morphology || bgcolor="#488ED3"|Normal
|-
| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal
|-
| [[Blood plasma|Plasma]] [[immunoglobulin]]s || bgcolor="#488ED3"|Normal
|-
| [[Haematology]] || bgcolor="#488ED3"|Normal<ref name="Haematology">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBWK/haematology-cbc/ |title=Haematology data for Prmt5 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Peripheral blood lymphocyte]]s || bgcolor="#488ED3"|Normal
|-
| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
|-
| Heart weight || bgcolor="#488ED3"|Normal
|-
| Brain histopathology || bgcolor="#488ED3"|Normal
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBWK/salmonella-challenge/ |title=''Salmonella'' infection data for Prmt5 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| ''[[Citrobacter]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Citrobacter'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBWK/citrobacter-challenge/ |title=''Citrobacter'' infection data for Prmt5 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal | doi = 10.1111/j.1755-3768.2010.4142.x | title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice | year = 2010 | author = Gerdin AK | journal = Acta Ophthalmologica | volume = 88 | pages =  925–7 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of PRMT5 function. A conditional [[knockout mouse]] line, called ''Prmt5<sup>tm2a(EUCOMM)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Prmt5 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4432368 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.<ref name="pmid21677750">{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–342 | year = 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | year = 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A Mouse for All Reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | year = 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref>
 
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism. | journal = Genome Biol | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}</ref> Twenty five tests were carried out on [[mutant]] mice and two significant abnormalities were observed.<ref name="mgp_reference" /> No [[homozygous]] mutant embryos were identified during gestation, and therefore none survived until [[weaning]]. The remaining tests were carried out on [[heterozygous]] mutant adult mice but no further abnormalities were observed.<ref name="mgp_reference" />
 
A conditional allele of Prmt5 in the mouse limb shows that it is essential for maintaining a progenitor population, as conditional mutants have limb defects <ref>Jacqueline L. Norrie, Qiang Li, Swanie Co, Bau-Lin Huang, Ding Ding, Jann C. Uy, Zhicheng Ji, Susan Mackem, Mark T. Bedford, Antonella Galli, Hongkai Ji, Steven A. Vokes
Development 2016 : doi: 10.1242/dev.140715</ref>
 
== Interactions ==
 
Protein arginine methyltransferase 5 has been shown to [[Protein-protein interaction|interact]] with:
* [[CLNS1A]],<ref name = pmid11756452/><ref name = pmid9556550>{{cite journal | vauthors = Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE | title = pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology | journal = J. Biol. Chem. | volume = 273 | issue = 18 | pages = 10811–4 | date = May 1998 | pmid = 9556550 | doi =  10.1074/jbc.273.18.10811}}</ref><ref name = pmid11713266>{{cite journal | vauthors = Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G, Rappsilber J, Mann M, Dreyfuss G | title = The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins | journal = Mol. Cell. Biol. | volume = 21 | issue = 24 | pages = 8289–300 | date = Dec 2001 | pmid = 11713266 | pmc = 99994 | doi = 10.1128/MCB.21.24.8289-8300.2001 }}</ref>
* [[Janus kinase 2]],<ref name = pmid10531356>{{cite journal | vauthors = Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S | title = The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity | journal = J. Biol. Chem. | volume = 274 | issue = 44 | pages = 31531–42 | date = Oct 1999 | pmid = 10531356 | doi =  10.1074/jbc.274.44.31531}}</ref>
* [[SNRPD3]],<ref name = pmid11713266/>
* [[SUPT5H]],<ref name = pmid12718890>{{cite journal | vauthors = Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB | title = Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties | journal = Mol. Cell | volume = 11 | issue = 4 | pages = 1055–66 | date = Apr 2003 | pmid = 12718890 | doi =  10.1016/s1097-2765(03)00101-1}}</ref> and
* [[WD repeat-containing protein 77]].<ref name = pmid11756452>{{cite journal | vauthors = Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, Dreyfuss G | title = A novel WD repeat protein component of the methylosome binds Sm proteins | journal = J. Biol. Chem. | volume = 277 | issue = 10 | pages = 8243–7 | date = Mar 2002 | pmid = 11756452 | doi = 10.1074/jbc.M109984200 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE | title = pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology. | journal = J. Biol. Chem. | volume = 273 | issue = 18 | pages = 10811–4 | year = 1998 | pmid = 9556550 | doi = 10.1074/jbc.273.18.10811 }}
| citations =
* {{cite journal | vauthors = Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S | title = The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. | journal = J. Biol. Chem. | volume = 274 | issue = 44 | pages = 31531–42 | year = 1999 | pmid = 10531356 | doi = 10.1074/jbc.274.44.31531 }}
*{{cite journal | author=Krapivinsky G, Pu W, Wickman K, ''et al.'' |title=pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 10811-4 |year= 1998 |pmid= 9556550 |doi= }}
* {{cite journal | vauthors = Schwärzler A, Kreienkamp HJ, Richter D | title = Interaction of the somatostatin receptor subtype 1 with the human homolog of the Shk1 kinase-binding protein from yeast. | journal = J. Biol. Chem. | volume = 275 | issue = 13 | pages = 9557–62 | year = 2000 | pmid = 10734105 | doi = 10.1074/jbc.275.13.9557 }}
*{{cite journal | author=Gilbreth M, Yang P, Bartholomeusz G, ''et al.'' |title=Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 25 |pages= 14781-6 |year= 1999 |pmid= 9843966 |doi= }}
* {{cite journal | vauthors = Rho J, Choi S, Seong YR, Cho WK, Kim SH, Im DS | title = Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. | journal = J. Biol. Chem. | volume = 276 | issue = 14 | pages = 11393–401 | year = 2001 | pmid = 11152681 | doi = 10.1074/jbc.M008660200 }}
*{{cite journal | author=Pollack BP, Kotenko SV, He W, ''et al.'' |title=The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. |journal=J. Biol. Chem. |volume=274 |issue= 44 |pages= 31531-42 |year= 1999 |pmid= 10531356 |doi= }}
* {{cite journal | vauthors = Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G, Rappsilber J, Mann M, Dreyfuss G | title = The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins. | journal = Mol. Cell. Biol. | volume = 21 | issue = 24 | pages = 8289–300 | year = 2001 | pmid = 11713266 | pmc = 99994 | doi = 10.1128/MCB.21.24.8289-8300.2001 }}
*{{cite journal | author=Schwärzler A, Kreienkamp HJ, Richter D |title=Interaction of the somatostatin receptor subtype 1 with the human homolog of the Shk1 kinase-binding protein from yeast. |journal=J. Biol. Chem. |volume=275 |issue= 13 |pages= 9557-62 |year= 2000 |pmid= 10734105 |doi= }}
* {{cite journal | vauthors = Brahms H, Meheus L, de Brabandere V, Fischer U, Lührmann R | title = Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein. | journal = RNA | volume = 7 | issue = 11 | pages = 1531–42 | year = 2001 | pmid = 11720283 | pmc = 1370196 | doi = 10.1017/S135583820101442X }}
*{{cite journal | author=Rho J, Choi S, Seong YR, ''et al.'' |title=Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. |journal=J. Biol. Chem. |volume=276 |issue= 14 |pages= 11393-401 |year= 2001 |pmid= 11152681 |doi= 10.1074/jbc.M008660200 }}
* {{cite journal | vauthors = Meister G, Eggert C, Bühler D, Brahms H, Kambach C, Fischer U | title = Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. | journal = Curr. Biol. | volume = 11 | issue = 24 | pages = 1990–4 | year = 2002 | pmid = 11747828 | doi = 10.1016/S0960-9822(01)00592-9 }}
*{{cite journal | author=Friesen WJ, Paushkin S, Wyce A, ''et al.'' |title=The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins. |journal=Mol. Cell. Biol. |volume=21 |issue= 24 |pages= 8289-300 |year= 2001 |pmid= 11713266 |doi= 10.1128/MCB.21.24.8289-8300.2001 }}
* {{cite journal | vauthors = Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, Dreyfuss G | title = A novel WD repeat protein component of the methylosome binds Sm proteins. | journal = J. Biol. Chem. | volume = 277 | issue = 10 | pages = 8243–7 | year = 2002 | pmid = 11756452 | doi = 10.1074/jbc.M109984200 }}
*{{cite journal | author=Brahms H, Meheus L, de Brabandere V, ''et al.'' |title=Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein. |journal=RNA |volume=7 |issue= 11 |pages= 1531-42 |year= 2001 |pmid= 11720283 |doi= }}
* {{cite journal | vauthors = Fabbrizio E, El Messaoudi S, Polanowska J, Paul C, Cook JR, Lee JH, Negre V, Rousset M, Pestka S, Le Cam A, Sardet C | title = Negative regulation of transcription by the type II arginine methyltransferase PRMT5. | journal = EMBO Rep. | volume = 3 | issue = 7 | pages = 641–5 | year = 2003 | pmid = 12101096 | pmc = 1084190 | doi = 10.1093/embo-reports/kvf136 }}
*{{cite journal | author=Meister G, Eggert C, Bühler D, ''et al.'' |title=Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. |journal=Curr. Biol. |volume=11 |issue= 24 |pages= 1990-4 |year= 2002 |pmid= 11747828 |doi= }}
* {{cite journal | vauthors = Jiang LQ, Wen SJ, Wang HY, Chen LY | title = Screening the proteins that interact with calpain in a human heart cDNA library using a yeast two-hybrid system. | journal = Hypertens. Res. | volume = 25 | issue = 4 | pages = 647–52 | year = 2003 | pmid = 12358155 | doi = 10.1291/hypres.25.647 }}
*{{cite journal | author=Friesen WJ, Wyce A, Paushkin S, ''et al.'' |title=A novel WD repeat protein component of the methylosome binds Sm proteins. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8243-7 |year= 2002 |pmid= 11756452 |doi= 10.1074/jbc.M109984200 }}
* {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. | journal = Nat. Biotechnol. | volume = 21 | issue = 5 | pages = 566–9 | year = 2004 | pmid = 12665801 | doi = 10.1038/nbt810 }}
*{{cite journal | author=Fabbrizio E, El Messaoudi S, Polanowska J, ''et al.'' |title=Negative regulation of transcription by the type II arginine methyltransferase PRMT5. |journal=EMBO Rep. |volume=3 |issue= 7 |pages= 641-5 |year= 2003 |pmid= 12101096 |doi= 10.1093/embo-reports/kvf136 }}
* {{cite journal | vauthors = Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB | title = Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. | journal = Mol. Cell | volume = 11 | issue = 4 | pages = 1055–66 | year = 2003 | pmid = 12718890 | doi = 10.1016/S1097-2765(03)00101-1 }}
*{{cite journal | author=Jiang LQ, Wen SJ, Wang HY, Chen LY |title=Screening the proteins that interact with calpain in a human heart cDNA library using a yeast two-hybrid system. |journal=Hypertens. Res. |volume=25 |issue= 4 |pages= 647-52 |year= 2003 |pmid= 12358155 |doi= }}
* {{cite journal | vauthors = Pal S, Yun R, Datta A, Lacomis L, Erdjument-Bromage H, Kumar J, Tempst P, Sif S | title = mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad. | journal = Mol. Cell. Biol. | volume = 23 | issue = 21 | pages = 7475–87 | year = 2003 | pmid = 14559996 | pmc = 207647 | doi = 10.1128/MCB.23.21.7475-7487.2003 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Yanagida M, Hayano T, Yamauchi Y, Shinkawa T, Natsume T, Isobe T, Takahashi N | title = Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins alpha 3 and beta 1 that is independent of its association with preribosomal ribonucleoprotein complexes. | journal = J. Biol. Chem. | volume = 279 | issue = 3 | pages = 1607–14 | year = 2004 | pmid = 14583623 | doi = 10.1074/jbc.M305604200 }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
* {{cite journal | vauthors = Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T | title = Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. | journal = Curr. Biol. | volume = 14 | issue = 16 | pages = 1436–50 | year = 2004 | pmid = 15324660 | doi = 10.1016/j.cub.2004.07.051 }}
*{{cite journal | author=Kwak YT, Guo J, Prajapati S, ''et al.'' |title=Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. |journal=Mol. Cell |volume=11 |issue= 4 |pages= 1055-66 |year= 2003 |pmid= 12718890 |doi= }}
* {{cite journal | vauthors = Miranda TB, Khusial P, Cook JR, Lee JH, Gunderson SI, Pestka S, Zieve GW, Clarke S | title = Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus. | journal = Biochem. Biophys. Res. Commun. | volume = 323 | issue = 2 | pages = 382–7 | year = 2004 | pmid = 15369763 | doi = 10.1016/j.bbrc.2004.08.107 }}
*{{cite journal | author=Pal S, Yun R, Datta A, ''et al.'' |title=mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad. |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7475-87 |year= 2003 |pmid= 14559996 |doi= }}
* {{cite journal | vauthors = Pal S, Vishwanath SN, Erdjument-Bromage H, Tempst P, Sif S | title = Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. | journal = Mol. Cell. Biol. | volume = 24 | issue = 21 | pages = 9630–45 | year = 2004 | pmid = 15485929 | pmc = 522266 | doi = 10.1128/MCB.24.21.9630-9645.2004 }}
*{{cite journal | author=Yanagida M, Hayano T, Yamauchi Y, ''et al.'' |title=Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins alpha 3 and beta 1 that is independent of its association with preribosomal ribonucleoprotein complexes. |journal=J. Biol. Chem. |volume=279 |issue= 3 |pages= 1607-14 |year= 2004 |pmid= 14583623 |doi= 10.1074/jbc.M305604200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Jin J, Smith FD, Stark C, ''et al.'' |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436-50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 }}
*{{cite journal  | author=Miranda TB, Khusial P, Cook JR, ''et al.'' |title=Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus. |journal=Biochem. Biophys. Res. Commun. |volume=323 |issue= 2 |pages= 382-7 |year= 2004 |pmid= 15369763 |doi= 10.1016/j.bbrc.2004.08.107 }}
*{{cite journal  | author=Pal S, Vishwanath SN, Erdjument-Bromage H, ''et al.'' |title=Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. |journal=Mol. Cell. Biol. |volume=24 |issue= 21 |pages= 9630-45 |year= 2004 |pmid= 15485929 |doi= 10.1128/MCB.24.21.9630-9645.2004 }}
}}
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{{protein-stub}}
[[Category:Genes mutated in mice]]

Latest revision as of 15:30, 8 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Protein arginine N-methyltransferase 5 is an enzyme that in humans is encoded by the PRMT5 gene.[1][2] PRMT5 symmetrically dimethylates H2AR3, H4R3, H3R2, and H3R8 in vivo, all of which are linked to a range of transcriptional regulatory events (Cell. Mol. Life Sci. (2015) 72:2041–2059 DOI 10.1007/s00018-015-1847-9)

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.[3]

Model organisms

Model organisms have been used in the study of PRMT5 function. A conditional knockout mouse line, called Prmt5tm2a(EUCOMM)Wtsi[9][10] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[11][12][13]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[7][14] Twenty five tests were carried out on mutant mice and two significant abnormalities were observed.[7] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice but no further abnormalities were observed.[7]

A conditional allele of Prmt5 in the mouse limb shows that it is essential for maintaining a progenitor population, as conditional mutants have limb defects [15]

Interactions

Protein arginine methyltransferase 5 has been shown to interact with:

References

  1. ↑ Gilbreth M, Yang P, Bartholomeusz G, Pimental RA, Kansra S, Gadiraju R, Marcus S (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.
  2. ↑ "Entrez Gene: PRMT5 protein arginine methyltransferase 5".
  3. ↑ Kim S, Gunesdogan, U, Zylicz JJ, Hackett, JA, Cougot, D, Bao, S, Lee, C, Dietmann, S, Allen, GE, Sngupta, R, Surani MA (Nov 2014). "PRMT5 Protects Genomic Integrity during Global DNA Demethylation in Primordial Germ Cells and Preimplantation Embryos". Molecular Cell. 56: 564–579. doi:10.1016/j.molcel.2014.10.003.
  4. ↑ "Haematology data for Prmt5". Wellcome Trust Sanger Institute.
  5. ↑ "Salmonella infection data for Prmt5". Wellcome Trust Sanger Institute.
  6. ↑ "Citrobacter infection data for Prmt5". Wellcome Trust Sanger Institute.
  7. ↑ 7.0 7.1 7.2 7.3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  8. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  9. ↑ "International Knockout Mouse Consortium".
  10. ↑ "Mouse Genome Informatics".
  11. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  12. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  13. ↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  14. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  15. ↑ Jacqueline L. Norrie, Qiang Li, Swanie Co, Bau-Lin Huang, Ding Ding, Jann C. Uy, Zhicheng Ji, Susan Mackem, Mark T. Bedford, Antonella Galli, Hongkai Ji, Steven A. Vokes Development 2016 : doi: 10.1242/dev.140715
  16. ↑ 16.0 16.1 Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, Dreyfuss G (Mar 2002). "A novel WD repeat protein component of the methylosome binds Sm proteins". J. Biol. Chem. 277 (10): 8243–7. doi:10.1074/jbc.M109984200. PMID 11756452.
  17. ↑ Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE (May 1998). "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology". J. Biol. Chem. 273 (18): 10811–4. doi:10.1074/jbc.273.18.10811. PMID 9556550.
  18. ↑ 18.0 18.1 Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G, Rappsilber J, Mann M, Dreyfuss G (Dec 2001). "The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins". Mol. Cell. Biol. 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. PMC 99994. PMID 11713266.
  19. ↑ Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S (Oct 1999). "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity". J. Biol. Chem. 274 (44): 31531–42. doi:10.1074/jbc.274.44.31531. PMID 10531356.
  20. ↑ Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB (Apr 2003). "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties". Mol. Cell. 11 (4): 1055–66. doi:10.1016/s1097-2765(03)00101-1. PMID 12718890.

Further reading

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