HUMAN:ANM6

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PRMT6 (synonyms: HRMT1L6)
Protein Name(s)	Protein arginine N-methyltransferase 6 Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6 Histone-arginine N-methyltransferase PRMT6
External Links
UniProt	Q96LA8
EMBL	AY043278 AK001421 AK295541 AL355539 CH471156 BC002729 BC063446 BC073866 BX475300
CCDS	CCDS41360.2
RefSeq	NP_060607.2
UniGene	Hs.26006
PDB	4HC4 4QPP 4QQK
PDBsum	4HC4 4QPP 4QQK
ProteinModelPortal	Q96LA8
SMR	Q96LA8
BioGrid	120469
IntAct	Q96LA8
MINT	MINT-6631342
STRING	9606.ENSP00000355145
BindingDB	Q96LA8
ChEMBL	CHEMBL1275221
GuidetoPHARMACOLOGY	1257
PhosphoSite	Q96LA8
DMDM	20137409
MaxQB	Q96LA8
PaxDb	Q96LA8
PRIDE	Q96LA8
DNASU	55170
Ensembl	ENST00000370078
GeneID	55170
KEGG	hsa:55170
UCSC	uc010ous.2
CTD	55170
GeneCards	GC01P107599
HGNC	HGNC:18241
HPA	HPA059424
MIM	608274
neXtProt	NX_Q96LA8
PharmGKB	PA134992775
eggNOG	COG0500
GeneTree	ENSGT00550000074406
HOGENOM	HOG000198521
HOVERGEN	HBG095907
InParanoid	Q96LA8
KO	K11437
OMA	GRFRFSC
OrthoDB	EOG74J97Z
PhylomeDB	Q96LA8
TreeFam	TF328817
Reactome	REACT_228108
SABIO-RK	Q96LA8
GeneWiki	PRMT6
GenomeRNAi	55170
NextBio	58949
PRO	PR:Q96LA8
Proteomes	UP000005640
Bgee	Q96LA8
CleanEx	HS_PRMT6
Genevestigator	Q96LA8
GO	GO:0005829 GO:0005634 GO:0042393 GO:0042054 GO:0070612 GO:0070611 GO:0044020 GO:0035242 GO:0035241 GO:0006284 GO:0034970 GO:0043985 GO:0016571 GO:0045892 GO:0019919 GO:0006351 GO:0016032
Gene3D	3.40.50.150
InterPro	IPR025799 IPR029063
PANTHER	PTHR11006
SUPFAM	SSF53335
PROSITE	PS51678

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0016274	protein-arginine N-methyltransferase activity	PMID:15596808^[1]	ECO:0000314			F	Figure 3	complete CACAO 3515
	GO:0016274	protein-arginine N-methyltransferase activity	PMID:17176473^[2]	ECO:0000314			F	Figure 4	complete CACAO 3525
	GO:0016274	protein-arginine N-methyltransferase activity	PMID:17267505^[3]	ECO:0000314			F	Figure 2	complete CACAO 3529
	GO:0008469	histone-arginine N-methyltransferase activity	PMID:23980157^[4]	ECO:0000314			F	Figure 2	complete CACAO 8577
enables	GO:0008469	histone-arginine N-methyltransferase activity	PMID:23980157^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070612	histone methyltransferase activity (H2A-R3 specific)	PMID:18079182^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070611	histone methyltransferase activity (H3-R2 specific)	PMID:18079182^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070611	histone methyltransferase activity (H3-R2 specific)	PMID:17898714^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:18079182^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0044020	histone methyltransferase activity (H4-R3 specific)	PMID:18079182^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:18079182^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:17898714^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042054	histone methyltransferase activity	PMID:19405910^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0035242	protein-arginine omega-N asymmetric methyltransferase activity	PMID:18079182^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0035242	protein-arginine omega-N asymmetric methyltransferase activity	PMID:17898714^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0035242	protein-arginine omega-N asymmetric methyltransferase activity	PMID:16157300^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0035242	protein-arginine omega-N asymmetric methyltransferase activity	PMID:11724789^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0035241	protein-arginine omega-N monomethyltransferase activity	PMID:16600869^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0035241	protein-arginine omega-N monomethyltransferase activity	PMID:16157300^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0035241	protein-arginine omega-N monomethyltransferase activity	PMID:11724789^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0034970	histone H3-R2 methylation	PMID:18079182^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0034970	histone H3-R2 methylation	PMID:17898714^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019919	peptidyl-arginine methylation, to asymmetrical-dimethyl arginine	PMID:18079182^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019919	peptidyl-arginine methylation, to asymmetrical-dimethyl arginine	PMID:17898714^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016571	histone methylation	PMID:19405910^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11724789^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0035242	protein-arginine omega-N asymmetric methyltransferase activity	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0037770 FB:FBgn0037834 MGI:MGI:107846 MGI:MGI:1913208 PANTHER:PTN000109455 RGD:62020 RGD:620413 SGD:S000000238 TAIR:locus:2010607 TAIR:locus:2077567 TAIR:locus:2154339 UniProtKB:Q7Q2B7 UniProtKB:Q96LA8 UniProtKB:Q99873 UniProtKB:Q9NR22 WB:WBGene00013766	F	Seeded From UniProt	complete
involved_in	GO:0034969	histone arginine methylation	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913208 MGI:MGI:2384879 PANTHER:PTN000109455 UniProtKB:Q582G4	P	Seeded From UniProt	complete
involved_in	GO:0019919	peptidyl-arginine methylation, to asymmetrical-dimethyl arginine	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0037770 FB:FBgn0037834 MGI:MGI:107846 PANTHER:PTN000109455 PomBase:SPAC890.07c PomBase:SPBC8D2.10c RGD:62020 RGD:620413 TAIR:locus:2010607 TAIR:locus:2077567 TAIR:locus:2154339 UniProtKB:Q7Q2B7 UniProtKB:Q96LA8 UniProtKB:Q9NR22 WB:WBGene00013766	P	Seeded From UniProt	complete
enables	GO:0008469	histone-arginine N-methyltransferase activity	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1316652 MGI:MGI:2139971 PANTHER:PTN000109455 RGD:62020 TAIR:locus:2010607 TAIR:locus:2077567 TAIR:locus:2154339 UniProtKB:C8V494 UniProtKB:C8VIM6 UniProtKB:Q86X55 UniProtKB:Q96LA8 UniProtKB:Q9NR22 UniProtKB:Q9NVM4 WB:WBGene00013766	F	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913208 PANTHER:PTN000109455 UniProtKB:Q7Q2B7	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913208 MGI:MGI:1919224 PANTHER:PTN000109455 RGD:62020 TAIR:locus:2010607 TAIR:locus:2051995 TAIR:locus:2082244 TAIR:locus:2134328 UniProtKB:P55345 UniProtKB:Q86X55 UniProtKB:Q9NVM4	C	Seeded From UniProt	complete
enables	GO:0008469	histone-arginine N-methyltransferase activity	PMID:22777353^[12]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008469	histone-arginine N-methyltransferase activity	PMID:19509293^[13]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	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:0043985	histone H4-R3 methylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0044020	P	Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6NZB1 ensembl:ENSMUSP00000140836	P	Seeded From UniProt	complete
involved_in	GO:0090398	cellular senescence	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6NZB1 ensembl:ENSMUSP00000140836	P	Seeded From UniProt	complete
involved_in	GO:0051572	negative regulation of histone H3-K4 methylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6NZB1 ensembl:ENSMUSP00000140836	P	Seeded From UniProt	complete
involved_in	GO:0035246	peptidyl-arginine N-methylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6NZB1 ensembl:ENSMUSP00000140836	P	Seeded From UniProt	complete
involved_in	GO:0034970	histone H3-R2 methylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6NZB1 ensembl:ENSMUSP00000140836	P	Seeded From UniProt	complete
enables	GO:0016274	protein-arginine N-methyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6NZB1 ensembl:ENSMUSP00000140836	F	Seeded From UniProt	complete
enables	GO:0008469	histone-arginine N-methyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6NZB1 ensembl:ENSMUSP00000140836	F	Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6NZB1 ensembl:ENSMUSP00000140836	F	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6NZB1 ensembl:ENSMUSP00000140836	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: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:IPR025799	F	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:16600869^[10]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045652	regulation of megakaryocyte differentiation	Reactome:R-HSA-8936459	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016274	protein-arginine N-methyltransferase activity	Reactome:R-HSA-5229203 Reactome:R-HSA-5205820	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008469	histone-arginine N-methyltransferase activity	Reactome:R-HSA-8937113	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-8937118 Reactome:R-HSA-8937113 Reactome:R-HSA-8937022 Reactome:R-HSA-8936989 Reactome:R-HSA-8936608 Reactome:R-HSA-8936599 Reactome:R-HSA-8936584 Reactome:R-HSA-8935732 Reactome:R-HSA-8935730 Reactome:R-HSA-5661126 Reactome:R-HSA-5229203 Reactome:R-HSA-5205824 Reactome:R-HSA-5205820 Reactome:R-HSA-5205798	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	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
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	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: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
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	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
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
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Notes

References

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

↑ Boulanger, MC et al. (2005) Methylation of Tat by PRMT6 regulates human immunodeficiency virus type 1 gene expression. J. Virol. 79 124-31 PubMed GONUTS page
↑ Invernizzi, CF et al. (2006) PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA. Retrovirology 3 93 PubMed GONUTS page
↑ Xie, B et al. (2007) Arginine methylation of the human immunodeficiency virus type 1 Tat protein by PRMT6 negatively affects Tat Interactions with both cyclin T1 and the Tat transactivation region. J. Virol. 81 4226-34 PubMed GONUTS page
↑ ^4.0 ^4.1 Casadio, F et al. (2013) H3R42me2a is a histone modification with positive transcriptional effects. Proc. Natl. Acad. Sci. U.S.A. 110 14894-9 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Hyllus, D et al. (2007) PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation. Genes Dev. 21 3369-80 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 Guccione, E et al. (2007) Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. Nature 449 933-7 PubMed GONUTS page
↑ ^7.0 ^7.1 Lakowski, TM & Frankel, A (2009) Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Biochem. J. 421 253-61 PubMed GONUTS page
↑ ^8.0 ^8.1 Miranda, TB et al. (2005) Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a. Biochem. Biophys. Res. Commun. 336 831-5 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Frankel, A et al. (2002) The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277 3537-43 PubMed GONUTS page
↑ ^10.0 ^10.1 El-Andaloussi, N et al. (2006) Arginine methylation regulates DNA polymerase beta. Mol. Cell 22 51-62 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Herglotz, J et al. (2013) Histone arginine methylation keeps RUNX1 target genes in an intermediate state. Oncogene 32 2565-75 PubMed GONUTS page
↑ Michaud-Levesque, J & Richard, S (2009) Thrombospondin-1 is a transcriptional repression target of PRMT6. J. Biol. Chem. 284 21338-46 PubMed GONUTS page

[PMID:15596808-1] Boulanger, MC et al. (2005) Methylation of Tat by PRMT6 regulates human immunodeficiency virus type 1 gene expression. J. Virol. 79 124-31 PubMed GONUTS page

[PMID:17176473-2] Invernizzi, CF et al. (2006) PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA. Retrovirology 3 93 PubMed GONUTS page

[PMID:17267505-3] Xie, B et al. (2007) Arginine methylation of the human immunodeficiency virus type 1 Tat protein by PRMT6 negatively affects Tat Interactions with both cyclin T1 and the Tat transactivation region. J. Virol. 81 4226-34 PubMed GONUTS page

[PMID:23980157-4] 4.0 ^4.1 Casadio, F et al. (2013) H3R42me2a is a histone modification with positive transcriptional effects. Proc. Natl. Acad. Sci. U.S.A. 110 14894-9 PubMed GONUTS page

[PMID:18079182-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Hyllus, D et al. (2007) PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation. Genes Dev. 21 3369-80 PubMed GONUTS page

[PMID:17898714-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 Guccione, E et al. (2007) Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. Nature 449 933-7 PubMed GONUTS page

[PMID:19405910-7] 7.0 ^7.1 Lakowski, TM & Frankel, A (2009) Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Biochem. J. 421 253-61 PubMed GONUTS page

[PMID:16157300-8] 8.0 ^8.1 Miranda, TB et al. (2005) Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a. Biochem. Biophys. Res. Commun. 336 831-5 PubMed GONUTS page

[PMID:11724789-9] 9.0 ^9.1 ^9.2 Frankel, A et al. (2002) The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277 3537-43 PubMed GONUTS page

[PMID:16600869-10] 10.0 ^10.1 El-Andaloussi, N et al. (2006) Arginine methylation regulates DNA polymerase beta. Mol. Cell 22 51-62 PubMed GONUTS page

[PMID:21873635-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 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:22777353-12] Herglotz, J et al. (2013) Histone arginine methylation keeps RUNX1 target genes in an intermediate state. Oncogene 32 2565-75 PubMed GONUTS page

[PMID:19509293-13] Michaud-Levesque, J & Richard, S (2009) Thrombospondin-1 is a transcriptional repression target of PRMT6. J. Biol. Chem. 284 21338-46 PubMed GONUTS page

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HUMAN:ANM6

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