Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein arginine N-methyltransferase 6 (EC 2.1.1.319) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6) (Histone-arginine N-methyltransferase PRMT6)

 ANM6_HUMAN              Reviewed;         375 AA.
Q96LA8; A3KME1; B4DID8; Q5T5Y5; Q6DKI4; Q9NVR8;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 154.
RecName: Full=Protein arginine N-methyltransferase 6;
EC=2.1.1.319 {ECO:0000269|PubMed:17898714, ECO:0000269|PubMed:18077460, ECO:0000269|PubMed:18079182, ECO:0000269|PubMed:19405910};
AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6;
AltName: Full=Histone-arginine N-methyltransferase PRMT6;
Name=PRMT6; Synonyms=HRMT1L6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND METHYLATION AT ARG-35.
TISSUE=Kidney;
PubMed=11724789; DOI=10.1074/jbc.M108786200;
Frankel A., Yadav N., Lee J., Branscombe T.L., Clarke S.,
Bedford M.T.;
"The novel human protein arginine N-methyltransferase PRMT6 is a
nuclear enzyme displaying unique substrate specificity.";
J. Biol. Chem. 277:3537-3543(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 25-375 (ISOFORM 1).
TISSUE=Hippocampus, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-194.
TISSUE=Blood, Eye, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 230-375 (ISOFORMS 1/2).
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
INTERACTION WITH EPB41L3.
PubMed=15334060; DOI=10.1038/sj.onc.1208057;
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.;
"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.";
Oncogene 23:7761-7771(2004).
[8]
INTERACTION WITH HIV-1 TAT.
PubMed=15596808; DOI=10.1128/JVI.79.1.124-131.2005;
Boulanger M.C., Liang C., Russell R.S., Lin R., Bedford M.T.,
Wainberg M.A., Richard S.;
"Methylation of Tat by PRMT6 regulates human immunodeficiency virus
type 1 gene expression.";
J. Virol. 79:124-131(2005).
[9]
FUNCTION, AND INTERACTION WITH HMGA1.
PubMed=16157300; DOI=10.1016/j.bbrc.2005.08.179;
Miranda T.B., Webb K.J., Edberg D.D., Reeves R., Clarke S.;
"Protein arginine methyltransferase 6 specifically methylates the
nonhistone chromatin protein HMGA1a.";
Biochem. Biophys. Res. Commun. 336:831-835(2005).
[10]
FUNCTION, AND INTERACTION WITH HMGA1.
PubMed=16159886; DOI=10.1074/jbc.M502458200;
Herrmann F., Lee J., Bedford M.T., Fackelmayer F.O.;
"Dynamics of human protein arginine methyltransferase 1(PRMT1) in
vivo.";
J. Biol. Chem. 280:38005-38010(2005).
[11]
FUNCTION, AND INTERACTION WITH POLB.
PubMed=16600869; DOI=10.1016/j.molcel.2006.02.013;
El-Andaloussi N., Valovka T., Toueille M., Steinacher R., Focke F.,
Gehrig P., Covic M., Hassa P.O., Schaer P., Huebscher U.,
Hottiger M.O.;
"Arginine methylation regulates DNA polymerase beta.";
Mol. Cell 22:51-62(2006).
[12]
INTERACTION WITH HIV-1 REV.
PubMed=17176473; DOI=10.1186/1742-4690-3-93;
Invernizzi C.F., Xie B., Richard S., Wainberg M.A.;
"PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA.";
Retrovirology 3:93-93(2006).
[13]
INTERACTION WITH HIV-1 NC.
PubMed=17415034; DOI=10.1097/QAD.0b013e32803277ae;
Invernizzi C.F., Xie B., Frankel F.A., Feldhammer M., Roy B.B.,
Richard S., Wainberg M.A.;
"Arginine methylation of the HIV-1 nucleocapsid protein results in its
diminished function.";
AIDS 21:795-805(2007).
[14]
FUNCTION, AND INTERACTION WITH HIV-1 TAT.
PubMed=17267505; DOI=10.1128/JVI.01888-06;
Xie B., Invernizzi C.F., Richard S., Wainberg M.A.;
"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. 81:4226-4234(2007).
[15]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 86-VAL--ASP-88.
PubMed=17898714; DOI=10.1038/nature06166;
Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M.,
Schuchlautz H., Luescher B., Amati B.;
"Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are
mutually exclusive.";
Nature 449:933-937(2007).
[16]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18079182; DOI=10.1101/gad.447007;
Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y.,
Hsieh J., Bauer U.M.;
"PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4
trimethylation.";
Genes Dev. 21:3369-3380(2007).
[17]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18077460; DOI=10.1074/jbc.C700192200;
Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J.,
Richard S., Bedford M.T.;
"Arginine methylation of the histone H3 tail impedes effector
binding.";
J. Biol. Chem. 283:3006-3010(2008).
[18]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18263580; DOI=10.1074/jbc.M710176200;
Lakowski T.M., Frankel A.;
"A kinetic study of human protein arginine N-methyltransferase 6
reveals a distributive mechanism.";
J. Biol. Chem. 283:10015-10025(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[20]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=19405910; DOI=10.1042/BJ20090268;
Lakowski T.M., Frankel A.;
"Kinetic analysis of human protein arginine N-methyltransferase 2:
formation of monomethyl- and asymmetric dimethyl-arginine residues on
histone H4.";
Biochem. J. 421:253-261(2009).
[21]
FUNCTION.
PubMed=19509293; DOI=10.1074/jbc.M109.005322;
Michaud-Levesque J., Richard S.;
"Thrombospondin-1 is a transcriptional repression target of PRMT6.";
J. Biol. Chem. 284:21338-21346(2009).
[22]
FUNCTION, INTERACTION WITH NCOA1, AND MUTAGENESIS OF 86-VAL--ASP-88.
PubMed=20047962; DOI=10.1093/nar/gkp1203;
Harrison M.J., Tang Y.H., Dowhan D.H.;
"Protein arginine methyltransferase 6 regulates multiple aspects of
gene expression.";
Nucleic Acids Res. 38:2201-2216(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
METHYLATION AT ARG-29; ARG-35 AND ARG-37, AND MUTAGENESIS OF ARG-35
AND 86-VAL--ASP-88.
PubMed=23866860; DOI=10.1186/1742-4690-10-73;
Singhroy D.N., Mesplede T., Sabbah A., Quashie P.K., Falgueyret J.P.,
Wainberg M.A.;
"Automethylation of protein arginine methyltransferase 6 (PRMT6)
regulates its stability and its anti-HIV-1 activity.";
Retrovirology 10:73-73(2013).
[26]
X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH
S-ADENOSYLHOMOCYSTEINE.
Structural genomics consortium (SGC);
"The crystal structure of human HMT1 HNRNP methyltransferase-like
protein 6 in complex with SAH.";
Submitted (OCT-2012) to the PDB data bank.
-!- FUNCTION: 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).
{ECO:0000250, ECO:0000269|PubMed:11724789,
ECO:0000269|PubMed:16157300, ECO:0000269|PubMed:16159886,
ECO:0000269|PubMed:16600869, ECO:0000269|PubMed:17267505,
ECO:0000269|PubMed:17898714, ECO:0000269|PubMed:18077460,
ECO:0000269|PubMed:18079182, ECO:0000269|PubMed:19405910,
ECO:0000269|PubMed:19509293, ECO:0000269|PubMed:20047962}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + [protein]-L-
arginine = 2 S-adenosyl-L-homocysteine + [protein]-
N(omega),N(omega)-dimethyl-L-arginine.
{ECO:0000269|PubMed:17898714, ECO:0000269|PubMed:18077460,
ECO:0000269|PubMed:18079182, ECO:0000269|PubMed:19405910}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=18.6 uM for AdoMet {ECO:0000269|PubMed:18263580};
KM=501 uM for WGGYSRGGYGGW peptide
{ECO:0000269|PubMed:18263580};
KM=183.7 uM for WGGYSR(MMA)GGYGGW monomethylated peptide
{ECO:0000269|PubMed:18263580};
Vmax=3.3 nmol/min/mg enzyme with AdoMet as substrate
{ECO:0000269|PubMed:18263580};
Vmax=1.8 nmol/min/mg enzyme with WGGYSRGGYGGW peptide as
substrate {ECO:0000269|PubMed:18263580};
Vmax=3.2 nmol/min/mg enzyme with WGGYSR(MMA)GGYGGW
monomethylated peptide as substrate
{ECO:0000269|PubMed:18263580};
-!- SUBUNIT: Interacts with (and methylates) HIV-1 Tat, Rev and
Nucleocapsid protein p7 (NC). Interacts with EPB41L3 and NCOA1.
{ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15596808,
ECO:0000269|PubMed:16157300, ECO:0000269|PubMed:16159886,
ECO:0000269|PubMed:16600869, ECO:0000269|PubMed:17176473,
ECO:0000269|PubMed:17267505, ECO:0000269|PubMed:17415034,
ECO:0000269|PubMed:20047962, ECO:0000269|Ref.26}.
-!- INTERACTION:
A8K932:-; NbExp=3; IntAct=EBI-912440, EBI-10174671;
Q6P047:C8orf74; NbExp=2; IntAct=EBI-912440, EBI-8466055;
Q9BXL8:CDCA4; NbExp=2; IntAct=EBI-912440, EBI-1773949;
Q96EY1:DNAJA3; NbExp=2; IntAct=EBI-912440, EBI-356767;
O14645:DNALI1; NbExp=2; IntAct=EBI-912440, EBI-395638;
Q9BQS8:FYCO1; NbExp=2; IntAct=EBI-912440, EBI-2869338;
Q8TE85:GRHL3; NbExp=2; IntAct=EBI-912440, EBI-8469396;
Q8NEC7:GSTCD; NbExp=2; IntAct=EBI-912440, EBI-8469616;
Q9BX10:GTPBP2; NbExp=2; IntAct=EBI-912440, EBI-6115579;
Q9UBX0:HESX1; NbExp=2; IntAct=EBI-912440, EBI-8470369;
P17096-1:HMGA1; NbExp=4; IntAct=EBI-912440, EBI-746854;
P52926:HMGA2; NbExp=2; IntAct=EBI-912440, EBI-912511;
Q9HAQ2:KIF9; NbExp=2; IntAct=EBI-912440, EBI-8472129;
Q9Y2M5:KLHL20; NbExp=2; IntAct=EBI-912440, EBI-714379;
Q96JB6:LOXL4; NbExp=2; IntAct=EBI-912440, EBI-749562;
Q9H204:MED28; NbExp=2; IntAct=EBI-912440, EBI-514199;
Q14995:NR1D2; NbExp=2; IntAct=EBI-912440, EBI-6144053;
P00973:OAS1; NbExp=2; IntAct=EBI-912440, EBI-3932815;
Q86SE9:PCGF5; NbExp=2; IntAct=EBI-912440, EBI-2827999;
O00231:PSMD11; NbExp=2; IntAct=EBI-912440, EBI-357816;
P50749:RASSF2; NbExp=2; IntAct=EBI-912440, EBI-960081;
Q9UGK8:SERGEF; NbExp=2; IntAct=EBI-912440, EBI-465368;
O15198:SMAD9; NbExp=2; IntAct=EBI-912440, EBI-748763;
Q96H20:SNF8; NbExp=2; IntAct=EBI-912440, EBI-747719;
Q96BD6:SPSB1; NbExp=2; IntAct=EBI-912440, EBI-2659201;
Q9Y365:STARD10; NbExp=2; IntAct=EBI-912440, EBI-4289836;
Q8N1K5:THEMIS; NbExp=2; IntAct=EBI-912440, EBI-2873538;
Q9Y3A6:TMED5; NbExp=2; IntAct=EBI-912440, EBI-7560959;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11724789}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96LA8-1; Sequence=Displayed;
Name=2;
IsoId=Q96LA8-2; Sequence=VSP_037465;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in kidney and testis.
{ECO:0000269|PubMed:11724789}.
-!- PTM: Automethylation enhances its stability and antiretroviral
activity.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. PRMT6 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU01015}.
-!- SEQUENCE CAUTION:
Sequence=AAH02729.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH63446.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA91681.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY043278; AAK85733.1; -; mRNA.
EMBL; AK001421; BAA91681.1; ALT_INIT; mRNA.
EMBL; AK295541; BAG58450.1; -; mRNA.
EMBL; AL355539; CAI19090.1; -; Genomic_DNA.
EMBL; CH471156; EAW51248.1; -; Genomic_DNA.
EMBL; BC002729; AAH02729.3; ALT_INIT; mRNA.
EMBL; BC063446; AAH63446.2; ALT_INIT; mRNA.
EMBL; BC073866; AAH73866.1; -; mRNA.
EMBL; BX475300; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS41360.2; -. [Q96LA8-1]
RefSeq; NP_060607.2; NM_018137.2. [Q96LA8-1]
UniGene; Hs.26006; -.
PDB; 4HC4; X-ray; 1.97 A; A=1-375.
PDB; 4QPP; X-ray; 2.52 A; A/B/C=1-375.
PDB; 4QQK; X-ray; 1.88 A; A=1-375.
PDB; 4Y2H; X-ray; 2.37 A; A/B=27-375.
PDB; 4Y30; X-ray; 2.10 A; A/B=25-375.
PDB; 5E8R; X-ray; 2.55 A; A/B=1-375.
PDB; 5EGS; X-ray; 2.15 A; A/B/C/D=1-375.
PDB; 5HZM; X-ray; 2.02 A; A=1-375.
PDB; 5WCF; X-ray; 1.98 A; A=1-375.
PDBsum; 4HC4; -.
PDBsum; 4QPP; -.
PDBsum; 4QQK; -.
PDBsum; 4Y2H; -.
PDBsum; 4Y30; -.
PDBsum; 5E8R; -.
PDBsum; 5EGS; -.
PDBsum; 5HZM; -.
PDBsum; 5WCF; -.
ProteinModelPortal; Q96LA8; -.
SMR; Q96LA8; -.
BioGrid; 120469; 126.
IntAct; Q96LA8; 86.
MINT; MINT-6631342; -.
STRING; 9606.ENSP00000359095; -.
BindingDB; Q96LA8; -.
ChEMBL; CHEMBL1275221; -.
GuidetoPHARMACOLOGY; 1257; -.
iPTMnet; Q96LA8; -.
PhosphoSitePlus; Q96LA8; -.
BioMuta; PRMT6; -.
DMDM; 20137409; -.
EPD; Q96LA8; -.
MaxQB; Q96LA8; -.
PaxDb; Q96LA8; -.
PeptideAtlas; Q96LA8; -.
PRIDE; Q96LA8; -.
DNASU; 55170; -.
Ensembl; ENST00000370078; ENSP00000359095; ENSG00000198890. [Q96LA8-1]
GeneID; 55170; -.
KEGG; hsa:55170; -.
UCSC; uc010ous.4; human. [Q96LA8-1]
CTD; 55170; -.
DisGeNET; 55170; -.
EuPathDB; HostDB:ENSG00000198890.7; -.
GeneCards; PRMT6; -.
HGNC; HGNC:18241; PRMT6.
HPA; HPA059424; -.
MIM; 608274; gene.
neXtProt; NX_Q96LA8; -.
OpenTargets; ENSG00000198890; -.
PharmGKB; PA134992775; -.
eggNOG; KOG1499; Eukaryota.
eggNOG; ENOG410XQYH; LUCA.
GeneTree; ENSGT00550000074406; -.
HOGENOM; HOG000198521; -.
HOVERGEN; HBG095907; -.
InParanoid; Q96LA8; -.
KO; K11437; -.
OMA; GVVFHWM; -.
OrthoDB; EOG091G0A0U; -.
PhylomeDB; Q96LA8; -.
TreeFam; TF328817; -.
BRENDA; 2.1.1.125; 2681.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
SABIO-RK; Q96LA8; -.
GeneWiki; PRMT6; -.
GenomeRNAi; 55170; -.
PRO; PR:Q96LA8; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000198890; -.
CleanEx; HS_PRMT6; -.
Genevisible; Q96LA8; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
GO; GO:0070612; F:histone methyltransferase activity (H2A-R3 specific); IDA:UniProtKB.
GO; GO:0070611; F:histone methyltransferase activity (H3-R2 specific); IDA:UniProtKB.
GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); IDA:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:CACAO.
GO; GO:0016274; F:protein-arginine N-methyltransferase activity; TAS:Reactome.
GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:UniProtKB.
GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB.
GO; GO:0006284; P:base-excision repair; TAS:UniProtKB.
GO; GO:0016049; P:cell growth; IEA:Ensembl.
GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
GO; GO:0034970; P:histone H3-R2 methylation; IDA:UniProtKB.
GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; DNA damage; DNA repair; Host-virus interaction;
Methylation; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase.
CHAIN 1 375 Protein arginine N-methyltransferase 6.
/FTId=PRO_0000212332.
DOMAIN 44 374 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
COMPBIAS 12 20 Poly-Gly.
ACT_SITE 155 155 {ECO:0000250}.
ACT_SITE 164 164 {ECO:0000250}.
BINDING 57 57 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 66 66 S-adenosyl-L-methionine.
BINDING 90 90 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 112 112 S-adenosyl-L-methionine.
BINDING 141 141 S-adenosyl-L-methionine.
MOD_RES 21 21 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 29 29 Omega-N-methylated arginine; by
autocatalysis.
{ECO:0000269|PubMed:23866860}.
MOD_RES 35 35 Omega-N-methylated arginine; by
autocatalysis.
{ECO:0000269|PubMed:23866860}.
MOD_RES 37 37 Omega-N-methylated arginine; by
autocatalysis.
{ECO:0000269|PubMed:23866860}.
VAR_SEQ 26 109 GAEREAALERPRRTKRERDQLYYECYSDVSVHEEMIADRVR
TDAYRLGILRNWAALRGKTVLDVGAGTGILSIFCAQAGARR
VY -> D (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037465.
VARIANT 194 194 A -> V (in dbSNP:rs2232016).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_057150.
MUTAGEN 35 35 R->A: Inhibits automethylation but does
not affect methylation of other proteins.
Reduces protein stability.
{ECO:0000269|PubMed:23866860}.
MUTAGEN 86 88 VLD->KLA: In PRMT6dn; abolishes histone
methyltransferase H3R2me2a and
transcriptional coactivator activities
and reduces protein stability. This
mutation abolishes automethylation.
{ECO:0000269|PubMed:17898714,
ECO:0000269|PubMed:20047962,
ECO:0000269|PubMed:23866860}.
HELIX 26 38 {ECO:0000244|PDB:4Y30}.
HELIX 41 49 {ECO:0000244|PDB:5EGS}.
HELIX 51 62 {ECO:0000244|PDB:4QQK}.
HELIX 64 75 {ECO:0000244|PDB:4QQK}.
HELIX 78 81 {ECO:0000244|PDB:4QQK}.
STRAND 85 90 {ECO:0000244|PDB:4QQK}.
HELIX 95 102 {ECO:0000244|PDB:4QQK}.
STRAND 106 112 {ECO:0000244|PDB:4QQK}.
HELIX 117 126 {ECO:0000244|PDB:4QQK}.
TURN 130 132 {ECO:0000244|PDB:4QQK}.
STRAND 133 138 {ECO:0000244|PDB:4QQK}.
TURN 140 142 {ECO:0000244|PDB:4QQK}.
STRAND 149 153 {ECO:0000244|PDB:4QQK}.
STRAND 158 163 {ECO:0000244|PDB:4QQK}.
HELIX 167 177 {ECO:0000244|PDB:4QQK}.
STRAND 178 186 {ECO:0000244|PDB:4QQK}.
STRAND 188 196 {ECO:0000244|PDB:4QQK}.
HELIX 199 206 {ECO:0000244|PDB:4QQK}.
HELIX 207 210 {ECO:0000244|PDB:4QQK}.
HELIX 211 215 {ECO:0000244|PDB:4QQK}.
HELIX 220 222 {ECO:0000244|PDB:4QQK}.
HELIX 223 231 {ECO:0000244|PDB:4QQK}.
STRAND 235 239 {ECO:0000244|PDB:4QQK}.
HELIX 243 245 {ECO:0000244|PDB:4QQK}.
STRAND 251 257 {ECO:0000244|PDB:4QQK}.
HELIX 263 269 {ECO:0000244|PDB:4QQK}.
STRAND 271 279 {ECO:0000244|PDB:4QQK}.
STRAND 283 296 {ECO:0000244|PDB:4QQK}.
TURN 299 302 {ECO:0000244|PDB:4Y30}.
STRAND 305 308 {ECO:0000244|PDB:4QQK}.
STRAND 320 331 {ECO:0000244|PDB:4QQK}.
STRAND 336 345 {ECO:0000244|PDB:4QQK}.
STRAND 352 361 {ECO:0000244|PDB:4QQK}.
STRAND 367 373 {ECO:0000244|PDB:4QQK}.
SEQUENCE 375 AA; 41938 MW; 40AAEC7342C08A38 CRC64;
MSQPKKRKLE SGGGGEGGEG TEEEDGAERE AALERPRRTK RERDQLYYEC YSDVSVHEEM
IADRVRTDAY RLGILRNWAA LRGKTVLDVG AGTGILSIFC AQAGARRVYA VEASAIWQQA
REVVRFNGLE DRVHVLPGPV ETVELPEQVD AIVSEWMGYG LLHESMLSSV LHARTKWLKE
GGLLLPASAE LFIAPISDQM LEWRLGFWSQ VKQHYGVDMS CLEGFATRCL MGHSEIVVQG
LSGEDVLARP QRFAQLELSR AGLEQELEAG VGGRFRCSCY GSAPMHGFAI WFQVTFPGGE
SEKPLVLSTS PFHPATHWKQ ALLYLNEPVQ VEQDTDVSGE ITLLPSRDNP RRLRVLLRYK
VGDQEEKTKD FAMED


Related products :

Catalog number Product name Quantity
18-003-42152 Protein arginine N-methyltransferase 3 - EC 2.1.1.-; Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3 Polyclonal 0.05 mg Aff Pur
EIAAB05333 CARM1,Coactivator-associated arginine methyltransferase 1,Histone-arginine methyltransferase CARM1,Homo sapiens,Human,PRMT4,Protein arginine N-methyltransferase 4
EIAAB05331 Carm1,Coactivator-associated arginine methyltransferase 1,Histone-arginine methyltransferase CARM1,Prmt4,Protein arginine N-methyltransferase 4,Rat,Rattus norvegicus
EIAAB05332 Carm1,Coactivator-associated arginine methyltransferase 1,Histone-arginine methyltransferase CARM1,Mouse,Mus musculus,Prmt4,Protein arginine N-methyltransferase 4
29-207 PRMT1 is a protein arginine methyltransferase that functions as a histone methyltransferase specific for H4.The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone me 0.1 mg
LF-PA40945 anti-Arginine Methyltransferase 6 (PRMT6) , Rabbit polyclonal to Arginine Methyltransferase 6 (PRMT6) , Isotype IgG, Host Rabbit 50 ul
PRMT6 PRMT6 Gene protein arginine methyltransferase 6
201-20-4508 PRMT6{protein arginine methyltransferase 6}rabbit.pAb 0.2ml
G2397 Protein arginine N-methyltransferase 6 (PRMT6), Mouse, ELISA Kit 96T
CSB-EL018735HU Human Protein arginine N-methyltransferase 6(PRMT6) ELISA kit 96T
CSB-EL018735MO Mouse Protein arginine N-methyltransferase 6(PRMT6) ELISA kit 96T
G2396 Protein arginine N-methyltransferase 6 (PRMT6), Human, ELISA Kit 96T
CSB-EL018735BO Bovine Protein arginine N-methyltransferase 6(PRMT6) ELISA kit 96T
G2395 Protein arginine N-methyltransferase 6 (PRMT6), Bovine, ELISA Kit 96T
CSB-EL018735HU Human Protein arginine N-methyltransferase 6(PRMT6) ELISA kit SpeciesHuman 96T
CSB-EL018735MO Mouse Protein arginine N-methyltransferase 6(PRMT6) ELISA kit SpeciesMouse 96T
CSB-EL018735BO Bovine Protein arginine N-methyltransferase 6(PRMT6) ELISA kit SpeciesBovine 96T
ANM6_MOUSE ELISA Kit FOR Protein arginine N-methyltransferase 6; organism: Mouse; gene name: Prmt6 96T
ANM6_HUMAN ELISA Kit FOR Protein arginine N-methyltransferase 6; organism: Human; gene name: PRMT6 96T
EIAAB37955 ERG-associated protein with SET domain,ESET,H3-K9-HMTase 4,Histone H3-K9 methyltransferase 4,Histone-lysine N-methyltransferase SETDB1,Homo sapiens,Human,KIAA0067,KMT1E,Lysine N-methyltransferase 1E,S
EIAAB37951 Histone-lysine N-methyltransferase SETD1A,Homo sapiens,hSET1A,Human,KIAA0339,KMT2F,Lysine N-methyltransferase 2F,SET domain-containing protein 1A,SET1,Set1_Ash2 histone methyltransferase complex subun
E2223Rb Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus,Rabbit
E2223Rb ELISA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus 96T
E2223m ELISA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Te 96T
U2223Rb CLIA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus, 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur