HUMAN:ANM5

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PRMT5 (synonyms: HRMT1L5, IBP72, JBP1, SKB1)
Protein Name(s)	Protein arginine N-methyltransferase 5 72 kDa ICln-binding protein Histone-arginine N-methyltransferase PRMT5 Jak-binding protein 1 Shk1 kinase-binding protein 1 homolog SKB1 homolog SKB1Hs Protein arginine N-methyltransferase 5, N-terminally processed
External Links
UniProt	O14744
EMBL	AF015913 AF167572 AK075251 AK301812 AK302240 CR456741 AB451246 AB451370 AL132780 CH471078 CH471078 CH471078 CH471078 BC005820 BC025979
CCDS	CCDS41922.1 CCDS61394.1 CCDS61395.1 CCDS61396.1 CCDS9579.1
PIR	T03842
RefSeq	NP_001034708.1 NP_001269882.1 NP_001269884.1 NP_001269885.1 NP_006100.2
UniGene	Hs.367854
PDB	4GQB
PDBsum	4GQB
ProteinModelPortal	O14744
SMR	O14744
BioGrid	115688
DIP	DIP-33172N
IntAct	O14744
MINT	MINT-1216859
STRING	9606.ENSP00000319169
BindingDB	O14744
ChEMBL	CHEMBL1795116
PhosphoSite	O14744
MaxQB	O14744
PaxDb	O14744
PeptideAtlas	O14744
PRIDE	O14744
DNASU	10419
Ensembl	ENST00000216350 ENST00000324366 ENST00000397440 ENST00000397441 ENST00000553897
GeneID	10419
KEGG	hsa:10419
UCSC	uc001whl.1 uc001whm.1 uc001whn.1
CTD	10419
GeneCards	GC14M023389
H-InvDB	HIX0011525
HGNC	HGNC:10894
HPA	CAB012459 HPA005525
MIM	604045
neXtProt	NX_O14744
PharmGKB	PA35794
eggNOG	NOG291156
GeneTree	ENSGT00390000001141
HOGENOM	HOG000175933
HOVERGEN	HBG057083
InParanoid	O14744
KO	K02516
OMA	SIPCSYT
OrthoDB	EOG7X6KZR
PhylomeDB	O14744
TreeFam	TF300626
Reactome	REACT_11066 REACT_228108
ChiTaRS	PRMT5
GeneWiki	Protein_arginine_methyltransferase_5
GenomeRNAi	10419
NextBio	35464858
PRO	PR:O14744
Proteomes	UP000005640
Bgee	O14744
CleanEx	HS_PRMT5
ExpressionAtlas	O14744
Genevestigator	O14744
GO	GO:0005737 GO:0005829 GO:0034709 GO:0005634 GO:0003682 GO:0001046 GO:0008469 GO:0008168 GO:0035243 GO:0043021 GO:0003714 GO:0008283 GO:0032922 GO:0042118 GO:0010467 GO:0043985 GO:0034660 GO:0000122 GO:0018216 GO:0019918 GO:0035246 GO:0007088 GO:0006355 GO:0016070 GO:0000387 GO:0006351
Gene3D	3.40.50.150
InterPro	IPR025799 IPR007857 IPR029063
PANTHER	PTHR10738
Pfam	PF05185
PIRSF	PIRSF015894
SUPFAM	SSF53335
PROSITE	PS51678

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005737	cytoplasm	PMID:22952863^[1]	ECO:0000314			C		Figure 1 shows PRMT5 localized in the cytoplasm	complete CACAO 7853
enables	GO:0008168	methyltransferase activity	PMID:19011621^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:19011621^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04637	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21081503^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21081503^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1904992	positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway	PMID:26554819^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P14416	P		Seeded From UniProt	complete
enables	GO:0016274	protein-arginine N-methyltransferase activity	PMID:26554819^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	has_input:(UniProtKB:P14416)	Seeded From UniProt	complete
involved_in	GO:0035246	peptidyl-arginine N-methylation	PMID:26554819^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0044020	histone methyltransferase activity (H4-R3 specific)	PMID:25284789^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0034709	methylosome	PMID:25284789^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008327	methyl-CpG binding	PMID:25284789^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006353	DNA-templated transcription, termination	PMID:26700805^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035097	histone methyltransferase complex	PMID:23048031^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0090161	Golgi ribbon formation	PMID:20421892^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016274	protein-arginine N-methyltransferase activity	PMID:20421892^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:20421892^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:22952863^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8CIG8	F		Seeded From UniProt	complete
enables	GO:0070888	E-box binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8CIG8	F		Seeded From UniProt	complete
involved_in	GO:0043985	histone H4-R3 methylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8CIG8	P		Seeded From UniProt	complete
involved_in	GO:0032922	circadian regulation of gene expression	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8CIG8	P		Seeded From UniProt	complete
involved_in	GO:0043985	histone H4-R3 methylation	PMID:18404153^[9]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043021	ribonucleoprotein complex binding	PMID:17709427^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P62318	F		Seeded From UniProt	complete
involved_in	GO:0042118	endothelial cell activation	PMID:22269951^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0035243	protein-arginine omega-N symmetric methyltransferase activity	PMID:17709427^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0034709	methylosome	PMID:18984161^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0018216	peptidyl-arginine methylation	PMID:17709427^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18984161^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:18404153^[9]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000387	spliceosomal snRNP assembly	PMID:17709427^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034969	histone arginine methylation	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000077429 WB:WBGene00016408	P		Seeded From UniProt	complete
enables	GO:0008469	histone-arginine N-methyltransferase activity	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000077429 UniProtKB:Q5BH46 WB:WBGene00016408	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000077429 TAIR:locus:2126276 UniProtKB:O14744	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1351645 PANTHER:PTN000077429 PomBase:SPBC16H5.11c UniProtKB:O14744 WB:WBGene00016408	C		Seeded From UniProt	complete
enables	GO:0035243	protein-arginine omega-N symmetric methyltransferase activity	PMID:19011621^[2]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:18495660^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0035246	peptidyl-arginine N-methylation	PMID:15369763^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008168	methyltransferase activity	PMID:15369763^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23071334^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O14744	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22365833^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O14744	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11756452^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O14744	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0019918	peptidyl-arginine methylation, to symmetrical-dimethyl arginine	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0035243	P		Seeded From UniProt	complete
involved_in	GO:0019918	peptidyl-arginine methylation, to symmetrical-dimethyl arginine	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0035243	P		Seeded From UniProt	complete
involved_in	GO:1903507	negative regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003714	P		Seeded From UniProt	complete
involved_in	GO:0097421	liver regeneration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A0E8 ensembl:ENSRNOP00000016302	P		Seeded From UniProt	complete
involved_in	GO:0070372	regulation of ERK1 and ERK2 cascade	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A0E8 ensembl:ENSRNOP00000016302	P		Seeded From UniProt	complete
involved_in	GO:0048714	positive regulation of oligodendrocyte differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A0E8 ensembl:ENSRNOP00000016302	P		Seeded From UniProt	complete
involved_in	GO:0045596	negative regulation of cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A0E8 ensembl:ENSRNOP00000016302	P		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A0E8 ensembl:ENSRNOP00000016302	F		Seeded From UniProt	complete
involved_in	GO:0044030	regulation of DNA methylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A0E8 ensembl:ENSRNOP00000016302	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A0E8 ensembl:ENSRNOP00000016302	C		Seeded From UniProt	complete
involved_in	GO:0006479	protein methylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A0E8 ensembl:ENSRNOP00000016302	P		Seeded From UniProt	complete
involved_in	GO:0006479	protein methylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007857 InterPro:IPR025799	P		Seeded From UniProt	complete
enables	GO:0008168	methyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007857 InterPro:IPR025799	F		Seeded From UniProt	complete
involved_in	GO:0035246	peptidyl-arginine N-methylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007857	P		Seeded From UniProt	complete
involved_in	GO:0007088	regulation of mitotic nuclear division	PMID:9843966^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	Reactome:R-HSA-5633007	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008469	histone-arginine N-methyltransferase activity	Reactome:R-HSA-5661117 Reactome:R-HSA-5216234 Reactome:R-HSA-5205861 Reactome:R-HSA-5205799	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-191790	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-6804383 Reactome:R-HSA-6804379 Reactome:R-HSA-5661117 Reactome:R-HSA-5218952 Reactome:R-HSA-5216234 Reactome:R-HSA-5205861 Reactome:R-HSA-5205799 Reactome:R-HSA-3215448 Reactome:R-HSA-3215426 Reactome:R-HSA-3215406 Reactome:R-HSA-3215391 Reactome:R-HSA-3215385	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000387	spliceosomal snRNP assembly	Reactome:R-HSA-191790	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008168	methyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0489	F		Seeded From UniProt	complete
involved_in	GO:0048511	rhythmic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0090	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
involved_in	GO:0032259	methylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0489	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333 UniProtKB-SubCell:SL-0132	C		Seeded From UniProt	complete
involved_in	GO:0006325	chromatin organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0156	P		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Gu, Z et al. (2012) Protein arginine methyltransferase 5 functions in opposite ways in the cytoplasm and nucleus of prostate cancer cells. PLoS ONE 7 e44033 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Jansson, M et al. (2008) Arginine methylation regulates the p53 response. Nat. Cell Biol. 10 1431-9 PubMed GONUTS page
↑ ^3.0 ^3.1 Guderian, G et al. (2011) RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity. J. Biol. Chem. 286 1976-86 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Likhite, N et al. (2015) The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling. Sci Signal 8 ra115 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Takai, H et al. (2014) 5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex. Cell Rep 9 48-60 PubMed GONUTS page
↑ Zhao, DY et al. (2016) SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination. Nature 529 48-53 PubMed GONUTS page
↑ Chittka, A et al. (2012) Transcription factor positive regulatory domain 4 (PRDM4) recruits protein arginine methyltransferase 5 (PRMT5) to mediate histone arginine methylation and control neural stem cell proliferation and differentiation. J. Biol. Chem. 287 42995-3006 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Zhou, Z et al. (2010) PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130. Cell Res. 20 1023-33 PubMed GONUTS page
↑ ^9.0 ^9.1 Lacroix, M et al. (2008) The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. EMBO Rep. 9 452-8 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Gonsalvez, GB et al. (2007) Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J. Cell Biol. 178 733-40 PubMed GONUTS page
↑ Bandyopadhyay, S et al. (2012) HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules. Mol. Cell. Biol. 32 1202-13 PubMed GONUTS page
↑ ^12.0 ^12.1 Chari, A et al. (2008) An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs. Cell 135 497-509 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Fronz, K et al. (2008) Promiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behavior. J. Biol. Chem. 283 20408-20 PubMed GONUTS page
↑ ^15.0 ^15.1 Miranda, TB et al. (2004) Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus. Biochem. Biophys. Res. Commun. 323 382-7 PubMed GONUTS page
↑ Antonysamy, S et al. (2012) Crystal structure of the human PRMT5:MEP50 complex. Proc. Natl. Acad. Sci. U.S.A. 109 17960-5 PubMed GONUTS page
↑ Hegele, A et al. (2012) Dynamic protein-protein interaction wiring of the human spliceosome. Mol. Cell 45 567-80 PubMed GONUTS page
↑ Friesen, WJ et al. (2002) A novel WD repeat protein component of the methylosome binds Sm proteins. J. Biol. Chem. 277 8243-7 PubMed GONUTS page
↑ Gilbreth, M et al. (1998) 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 14781-6 PubMed GONUTS page

[PMID:22952863-1] 1.0 ^1.1 Gu, Z et al. (2012) Protein arginine methyltransferase 5 functions in opposite ways in the cytoplasm and nucleus of prostate cancer cells. PLoS ONE 7 e44033 PubMed GONUTS page

[PMID:19011621-2] 2.0 ^2.1 ^2.2 Jansson, M et al. (2008) Arginine methylation regulates the p53 response. Nat. Cell Biol. 10 1431-9 PubMed GONUTS page

[PMID:21081503-3] 3.0 ^3.1 Guderian, G et al. (2011) RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity. J. Biol. Chem. 286 1976-86 PubMed GONUTS page

[PMID:26554819-4] 4.0 ^4.1 ^4.2 Likhite, N et al. (2015) The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling. Sci Signal 8 ra115 PubMed GONUTS page

[PMID:25284789-5] 5.0 ^5.1 ^5.2 Takai, H et al. (2014) 5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex. Cell Rep 9 48-60 PubMed GONUTS page

[PMID:26700805-6] Zhao, DY et al. (2016) SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination. Nature 529 48-53 PubMed GONUTS page

[PMID:23048031-7] Chittka, A et al. (2012) Transcription factor positive regulatory domain 4 (PRDM4) recruits protein arginine methyltransferase 5 (PRMT5) to mediate histone arginine methylation and control neural stem cell proliferation and differentiation. J. Biol. Chem. 287 42995-3006 PubMed GONUTS page

[PMID:20421892-8] 8.0 ^8.1 ^8.2 Zhou, Z et al. (2010) PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130. Cell Res. 20 1023-33 PubMed GONUTS page

[PMID:18404153-9] 9.0 ^9.1 Lacroix, M et al. (2008) The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. EMBO Rep. 9 452-8 PubMed GONUTS page

[PMID:17709427-10] 10.0 ^10.1 ^10.2 ^10.3 Gonsalvez, GB et al. (2007) Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J. Cell Biol. 178 733-40 PubMed GONUTS page

[PMID:22269951-11] Bandyopadhyay, S et al. (2012) HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules. Mol. Cell. Biol. 32 1202-13 PubMed GONUTS page

[PMID:18984161-12] 12.0 ^12.1 Chari, A et al. (2008) An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs. Cell 135 497-509 PubMed GONUTS page

[PMID:21873635-13] 13.0 ^13.1 ^13.2 ^13.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:18495660-14] Fronz, K et al. (2008) Promiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behavior. J. Biol. Chem. 283 20408-20 PubMed GONUTS page

[PMID:15369763-15] 15.0 ^15.1 Miranda, TB et al. (2004) Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus. Biochem. Biophys. Res. Commun. 323 382-7 PubMed GONUTS page

[PMID:23071334-16] Antonysamy, S et al. (2012) Crystal structure of the human PRMT5:MEP50 complex. Proc. Natl. Acad. Sci. U.S.A. 109 17960-5 PubMed GONUTS page

[PMID:22365833-17] Hegele, A et al. (2012) Dynamic protein-protein interaction wiring of the human spliceosome. Mol. Cell 45 567-80 PubMed GONUTS page

[PMID:11756452-18] Friesen, WJ et al. (2002) A novel WD repeat protein component of the methylosome binds Sm proteins. J. Biol. Chem. 277 8243-7 PubMed GONUTS page

[PMID:9843966-19] Gilbreth, M et al. (1998) 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 14781-6 PubMed GONUTS page

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HUMAN:ANM5

Contents

Annotations

Notes

References

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