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Protein

Protein arginine N-methyltransferase 6

Gene

PRMT6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53. Repression of TP53 blocks cellular senescence (By similarity). Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes fasting-induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator. May play a role in innate immunity against HIV-1 in case of infection by methylating and impairing the function of various HIV-1 proteins such as Tat, Rev and Nucleocapsid protein p7 (NC).By similarity11 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.4 Publications

Kineticsi

  1. KM=18.6 µM for AdoMet1 Publication
  2. KM=501 µM for WGGYSRGGYGGW peptide1 Publication
  3. KM=183.7 µM for WGGYSR(MMA)GGYGGW monomethylated peptide1 Publication
  1. Vmax=3.3 nmol/min/mg enzyme with AdoMet as substrate1 Publication
  2. Vmax=1.8 nmol/min/mg enzyme with WGGYSRGGYGGW peptide as substrate1 Publication
  3. Vmax=3.2 nmol/min/mg enzyme with WGGYSR(MMA)GGYGGW monomethylated peptide as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571S-adenosyl-L-methionineBy similarity
Binding sitei66 – 661S-adenosyl-L-methionine
Binding sitei90 – 901S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei112 – 1121S-adenosyl-L-methionine
Binding sitei141 – 1411S-adenosyl-L-methionine
Active sitei155 – 1551By similarity
Active sitei164 – 1641By similarity

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • histone-arginine N-methyltransferase activity Source: CACAO
  • histone binding Source: UniProtKB
  • histone methyltransferase activity Source: UniProtKB
  • histone methyltransferase activity (H2A-R3 specific) Source: UniProtKB
  • histone methyltransferase activity (H3-R2 specific) Source: UniProtKB
  • histone methyltransferase activity (H4-R3 specific) Source: UniProtKB
  • protein-arginine N-methyltransferase activity Source: Reactome
  • protein-arginine omega-N asymmetric methyltransferase activity Source: UniProtKB
  • protein-arginine omega-N monomethyltransferase activity Source: UniProtKB

GO - Biological processi

  • base-excision repair Source: UniProtKB
  • cell growth Source: Ensembl
  • cellular senescence Source: Ensembl
  • histone H3-R2 methylation Source: UniProtKB
  • histone methylation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.125. 2681.
ReactomeiR-HSA-3214858. RMTs methylate histone arginines.
SABIO-RKQ96LA8.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 6 (EC:2.1.1.3194 Publications)
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6
Histone-arginine N-methyltransferase PRMT6
Gene namesi
Name:PRMT6
Synonyms:HRMT1L6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18241. PRMT6.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351R → A: Inhibits automethylation but does not affect methylation of other proteins. Reduces protein stability. 1 Publication
Mutagenesisi86 – 883VLD → KLA in PRMT6dn; abolishes histone methyltransferase H3R2me2a and transcriptional coactivator activities and reduces protein stability. This mutation abolishes automethylation. 3 Publications

Organism-specific databases

PharmGKBiPA134992775.

Chemistry

ChEMBLiCHEMBL1275221.
GuidetoPHARMACOLOGYi1257.

Polymorphism and mutation databases

BioMutaiPRMT6.
DMDMi20137409.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Protein arginine N-methyltransferase 6PRO_0000212332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphothreonineCombined sources
Modified residuei29 – 291Omega-N-methylated arginine; by autocatalysis1 Publication
Modified residuei35 – 351Omega-N-methylated arginine; by autocatalysis1 Publication
Modified residuei37 – 371Omega-N-methylated arginine; by autocatalysis1 Publication

Post-translational modificationi

Automethylation enhances its stability and antiretroviral activity.

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ96LA8.
MaxQBiQ96LA8.
PaxDbiQ96LA8.
PeptideAtlasiQ96LA8.
PRIDEiQ96LA8.

PTM databases

iPTMnetiQ96LA8.
PhosphoSiteiQ96LA8.

Expressioni

Tissue specificityi

Highly expressed in kidney and testis.1 Publication

Gene expression databases

BgeeiQ96LA8.
CleanExiHS_PRMT6.
GenevisibleiQ96LA8. HS.

Organism-specific databases

HPAiHPA059424.

Interactioni

Subunit structurei

Interacts with (and methylates) HIV-1 Tat, Rev and Nucleocapsid protein p7 (NC). Interacts with EPB41L3 and NCOA1.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A8K9323EBI-912440,EBI-10174671
C8orf74Q6P0472EBI-912440,EBI-8466055
CDCA4Q9BXL82EBI-912440,EBI-1773949
DNAJA3Q96EY12EBI-912440,EBI-356767
DNALI1O146452EBI-912440,EBI-395638
FYCO1Q9BQS82EBI-912440,EBI-2869338
GRHL3Q8TE852EBI-912440,EBI-8469396
GSTCDQ8NEC72EBI-912440,EBI-8469616
GTPBP2Q9BX102EBI-912440,EBI-6115579
HESX1Q9UBX02EBI-912440,EBI-8470369
HMGA1P17096-14EBI-912440,EBI-746854
HMGA2P529262EBI-912440,EBI-912511
KIF9Q9HAQ22EBI-912440,EBI-8472129
KLHL20Q9Y2M52EBI-912440,EBI-714379
LOXL4Q96JB62EBI-912440,EBI-749562
MED28Q9H2042EBI-912440,EBI-514199
NR1D2Q149952EBI-912440,EBI-6144053
OAS1P009732EBI-912440,EBI-3932815
PCGF5Q86SE92EBI-912440,EBI-2827999
PSMD11O002312EBI-912440,EBI-357816
RASSF2P507492EBI-912440,EBI-960081
SERGEFQ9UGK82EBI-912440,EBI-465368
SMAD9O151982EBI-912440,EBI-748763
SNF8Q96H202EBI-912440,EBI-747719
SPSB1Q96BD62EBI-912440,EBI-2659201
STARD10Q9Y3652EBI-912440,EBI-4289836
THEMISQ8N1K52EBI-912440,EBI-2873538
TMED5Q9Y3A62EBI-912440,EBI-7560959

GO - Molecular functioni

  • histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120469. 122 interactions.
IntActiQ96LA8. 85 interactions.
MINTiMINT-6631342.
STRINGi9606.ENSP00000359095.

Chemistry

BindingDBiQ96LA8.

Structurei

Secondary structure

1
375
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 3813Combined sources
Helixi41 – 499Combined sources
Helixi51 – 6212Combined sources
Helixi64 – 7512Combined sources
Helixi78 – 814Combined sources
Beta strandi85 – 906Combined sources
Helixi95 – 1028Combined sources
Beta strandi106 – 1127Combined sources
Helixi117 – 12610Combined sources
Turni130 – 1323Combined sources
Beta strandi133 – 1386Combined sources
Turni140 – 1423Combined sources
Beta strandi149 – 1535Combined sources
Beta strandi158 – 1636Combined sources
Helixi167 – 17711Combined sources
Beta strandi178 – 1869Combined sources
Beta strandi188 – 1969Combined sources
Helixi199 – 2068Combined sources
Helixi207 – 2104Combined sources
Helixi211 – 2155Combined sources
Helixi220 – 2223Combined sources
Helixi223 – 2319Combined sources
Beta strandi235 – 2395Combined sources
Helixi243 – 2453Combined sources
Beta strandi251 – 2577Combined sources
Helixi263 – 2697Combined sources
Beta strandi271 – 2799Combined sources
Beta strandi283 – 29614Combined sources
Turni299 – 3024Combined sources
Beta strandi305 – 3084Combined sources
Beta strandi320 – 33112Combined sources
Beta strandi336 – 34510Combined sources
Beta strandi352 – 36110Combined sources
Beta strandi367 – 3737Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HC4X-ray1.97A1-375[»]
4QPPX-ray2.52A/B/C1-375[»]
4QQKX-ray1.88A1-375[»]
4Y2HX-ray2.37A/B27-375[»]
4Y30X-ray2.10A/B25-375[»]
5E8RX-ray2.55A/B1-375[»]
5EGSX-ray2.15A/B/C/D1-375[»]
5HZMX-ray2.02A1-375[»]
ProteinModelPortaliQ96LA8.
SMRiQ96LA8. Positions 25-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 374331SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 209Poly-Gly

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT6 subfamily.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG095907.
InParanoidiQ96LA8.
KOiK11437.
OMAiGRFRFSC.
OrthoDBiEOG74J97Z.
PhylomeDBiQ96LA8.
TreeFamiTF328817.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96LA8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSQPKKRKLE SGGGGEGGEG TEEEDGAERE AALERPRRTK RERDQLYYEC
60 70 80 90 100
YSDVSVHEEM IADRVRTDAY RLGILRNWAA LRGKTVLDVG AGTGILSIFC
110 120 130 140 150
AQAGARRVYA VEASAIWQQA REVVRFNGLE DRVHVLPGPV ETVELPEQVD
160 170 180 190 200
AIVSEWMGYG LLHESMLSSV LHARTKWLKE GGLLLPASAE LFIAPISDQM
210 220 230 240 250
LEWRLGFWSQ VKQHYGVDMS CLEGFATRCL MGHSEIVVQG LSGEDVLARP
260 270 280 290 300
QRFAQLELSR AGLEQELEAG VGGRFRCSCY GSAPMHGFAI WFQVTFPGGE
310 320 330 340 350
SEKPLVLSTS PFHPATHWKQ ALLYLNEPVQ VEQDTDVSGE ITLLPSRDNP
360 370
RRLRVLLRYK VGDQEEKTKD FAMED
Length:375
Mass (Da):41,938
Last modified:December 1, 2001 - v1
Checksum:i40AAEC7342C08A38
GO
Isoform 2 (identifier: Q96LA8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-109: GAEREAALER...CAQAGARRVY → D

Note: No experimental confirmation available.
Show »
Length:292
Mass (Da):32,509
Checksum:i9E6341283024795C
GO

Sequence cautioni

The sequence AAH02729.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH63446.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA91681.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti194 – 1941A → V.1 Publication
Corresponds to variant rs2232016 [ dbSNP | Ensembl ].
VAR_057150

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 10984GAERE…ARRVY → D in isoform 2. 1 PublicationVSP_037465Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY043278 mRNA. Translation: AAK85733.1.
AK001421 mRNA. Translation: BAA91681.1. Different initiation.
AK295541 mRNA. Translation: BAG58450.1.
AL355539 Genomic DNA. Translation: CAI19090.1.
CH471156 Genomic DNA. Translation: EAW51248.1.
BC002729 mRNA. Translation: AAH02729.3. Different initiation.
BC063446 mRNA. Translation: AAH63446.2. Different initiation.
BC073866 mRNA. Translation: AAH73866.1.
BX475300 mRNA. No translation available.
CCDSiCCDS41360.2. [Q96LA8-1]
RefSeqiNP_060607.2. NM_018137.2. [Q96LA8-1]
UniGeneiHs.26006.

Genome annotation databases

EnsembliENST00000370078; ENSP00000359095; ENSG00000198890. [Q96LA8-1]
GeneIDi55170.
KEGGihsa:55170.
UCSCiuc010ous.4. human. [Q96LA8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY043278 mRNA. Translation: AAK85733.1.
AK001421 mRNA. Translation: BAA91681.1. Different initiation.
AK295541 mRNA. Translation: BAG58450.1.
AL355539 Genomic DNA. Translation: CAI19090.1.
CH471156 Genomic DNA. Translation: EAW51248.1.
BC002729 mRNA. Translation: AAH02729.3. Different initiation.
BC063446 mRNA. Translation: AAH63446.2. Different initiation.
BC073866 mRNA. Translation: AAH73866.1.
BX475300 mRNA. No translation available.
CCDSiCCDS41360.2. [Q96LA8-1]
RefSeqiNP_060607.2. NM_018137.2. [Q96LA8-1]
UniGeneiHs.26006.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HC4X-ray1.97A1-375[»]
4QPPX-ray2.52A/B/C1-375[»]
4QQKX-ray1.88A1-375[»]
4Y2HX-ray2.37A/B27-375[»]
4Y30X-ray2.10A/B25-375[»]
5E8RX-ray2.55A/B1-375[»]
5EGSX-ray2.15A/B/C/D1-375[»]
5HZMX-ray2.02A1-375[»]
ProteinModelPortaliQ96LA8.
SMRiQ96LA8. Positions 25-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120469. 122 interactions.
IntActiQ96LA8. 85 interactions.
MINTiMINT-6631342.
STRINGi9606.ENSP00000359095.

Chemistry

BindingDBiQ96LA8.
ChEMBLiCHEMBL1275221.
GuidetoPHARMACOLOGYi1257.

PTM databases

iPTMnetiQ96LA8.
PhosphoSiteiQ96LA8.

Polymorphism and mutation databases

BioMutaiPRMT6.
DMDMi20137409.

Proteomic databases

EPDiQ96LA8.
MaxQBiQ96LA8.
PaxDbiQ96LA8.
PeptideAtlasiQ96LA8.
PRIDEiQ96LA8.

Protocols and materials databases

DNASUi55170.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370078; ENSP00000359095; ENSG00000198890. [Q96LA8-1]
GeneIDi55170.
KEGGihsa:55170.
UCSCiuc010ous.4. human. [Q96LA8-1]

Organism-specific databases

CTDi55170.
GeneCardsiPRMT6.
HGNCiHGNC:18241. PRMT6.
HPAiHPA059424.
MIMi608274. gene.
neXtProtiNX_Q96LA8.
PharmGKBiPA134992775.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG095907.
InParanoidiQ96LA8.
KOiK11437.
OMAiGRFRFSC.
OrthoDBiEOG74J97Z.
PhylomeDBiQ96LA8.
TreeFamiTF328817.

Enzyme and pathway databases

BRENDAi2.1.1.125. 2681.
ReactomeiR-HSA-3214858. RMTs methylate histone arginines.
SABIO-RKQ96LA8.

Miscellaneous databases

GeneWikiiPRMT6.
GenomeRNAii55170.
PROiQ96LA8.
SOURCEiSearch...

Gene expression databases

BgeeiQ96LA8.
CleanExiHS_PRMT6.
GenevisibleiQ96LA8. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity."
    Frankel A., Yadav N., Lee J., Branscombe T.L., Clarke S., Bedford M.T.
    J. Biol. Chem. 277:3537-3543(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, METHYLATION AT ARG-35.
    Tissue: Kidney.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-375 (ISOFORM 1).
    Tissue: Hippocampus and Teratocarcinoma.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-194.
    Tissue: Blood, Eye and Placenta.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 230-375 (ISOFORMS 1/2).
  7. "DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo."
    Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A., Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.
    Oncogene 23:7761-7771(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPB41L3.
  8. "Methylation of Tat by PRMT6 regulates human immunodeficiency virus type 1 gene expression."
    Boulanger M.C., Liang C., Russell R.S., Lin R., Bedford M.T., Wainberg M.A., Richard S.
    J. Virol. 79:124-131(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  9. "Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a."
    Miranda T.B., Webb K.J., Edberg D.D., Reeves R., Clarke S.
    Biochem. Biophys. Res. Commun. 336:831-835(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HMGA1.
  10. "Dynamics of human protein arginine methyltransferase 1(PRMT1) in vivo."
    Herrmann F., Lee J., Bedford M.T., Fackelmayer F.O.
    J. Biol. Chem. 280:38005-38010(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HMGA1.
  11. Cited for: FUNCTION, INTERACTION WITH POLB.
  12. "PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA."
    Invernizzi C.F., Xie B., Richard S., Wainberg M.A.
    Retrovirology 3:93-93(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 REV.
  13. "Arginine methylation of the HIV-1 nucleocapsid protein results in its diminished function."
    Invernizzi C.F., Xie B., Frankel F.A., Feldhammer M., Roy B.B., Richard S., Wainberg M.A.
    AIDS 21:795-805(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 NC.
  14. "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."
    Xie B., Invernizzi C.F., Richard S., Wainberg M.A.
    J. Virol. 81:4226-4234(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIV-1 TAT.
  15. "Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive."
    Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M., Schuchlautz H., Luescher B., Amati B.
    Nature 449:933-937(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF 86-VAL--ASP-88.
  16. "PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation."
    Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y., Hsieh J., Bauer U.M.
    Genes Dev. 21:3369-3380(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  17. "Arginine methylation of the histone H3 tail impedes effector binding."
    Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J., Richard S., Bedford M.T.
    J. Biol. Chem. 283:3006-3010(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  18. "A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism."
    Lakowski T.M., Frankel A.
    J. Biol. Chem. 283:10015-10025(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4."
    Lakowski T.M., Frankel A.
    Biochem. J. 421:253-261(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  21. "Thrombospondin-1 is a transcriptional repression target of PRMT6."
    Michaud-Levesque J., Richard S.
    J. Biol. Chem. 284:21338-21346(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Protein arginine methyltransferase 6 regulates multiple aspects of gene expression."
    Harrison M.J., Tang Y.H., Dowhan D.H.
    Nucleic Acids Res. 38:2201-2216(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCOA1, MUTAGENESIS OF 86-VAL--ASP-88.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  25. "Automethylation of protein arginine methyltransferase 6 (PRMT6) regulates its stability and its anti-HIV-1 activity."
    Singhroy D.N., Mesplede T., Sabbah A., Quashie P.K., Falgueyret J.P., Wainberg M.A.
    Retrovirology 10:73-73(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-29; ARG-35 AND ARG-37, MUTAGENESIS OF ARG-35 AND 86-VAL--ASP-88.
  26. "The crystal structure of human HMT1 HNRNP methyltransferase-like protein 6 in complex with SAH."
    Structural genomics consortium (SGC)
    Submitted (OCT-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH S-ADENOSYLHOMOCYSTEINE.

Entry informationi

Entry nameiANM6_HUMAN
AccessioniPrimary (citable) accession number: Q96LA8
Secondary accession number(s): A3KME1
, B4DID8, Q5T5Y5, Q6DKI4, Q9NVR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.