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Protein arginine N-methyltransferase 3 (EC 2.1.1.-) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3)

 ANM3_HUMAN              Reviewed;         531 AA.
O60678; B4DUC7;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
25-OCT-2017, entry version 160.
RecName: Full=Protein arginine N-methyltransferase 3;
EC=2.1.1.-;
AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3;
Name=PRMT3; Synonyms=HRMT1L3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ASN-508.
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASN-508.
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-531 (ISOFORM 1), AND VARIANT ASN-508.
PubMed=9642256; DOI=10.1074/jbc.273.27.16935;
Tang J., Gary J.D., Clarke S., Herschman H.R.;
"PRMT 3, a type I protein arginine N-methyltransferase that differs
from PRMT1 in its oligomerization, subcellular localization, substrate
specificity, and regulation.";
J. Biol. Chem. 273:16935-16945(1998).
[5]
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
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).
[11]
PHOSPHORYLATION AT SER-25 AND SER-27, MUTAGENESIS OF TYR-87, ABSENCE
OF PHOSPHORYLATION AT TYR-87, AND INTERACTION WITH RPS2.
PubMed=21059412; DOI=10.1016/j.bbapap.2010.10.011;
Handrkova H., Petrak J., Halada P., Pospisilova D., Cmejla R.;
"Tyrosine 87 is vital for the activity of human protein arginine
methyltransferase 3 (PRMT3).";
Biochim. Biophys. Acta 1814:277-282(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-27 AND SER-171,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[16]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 211-531 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE.
Structural genomics consortium (SGC);
"The crystal structure of human HMT1 HNRNP methyltransferase-like 3 in
complex with SAH.";
Submitted (MAR-2006) to the PDB data bank.
-!- FUNCTION: Methylates (mono and asymmetric dimethylation) the
guanidino nitrogens of arginyl residues in some proteins.
-!- ENZYME REGULATION: Inhibited by N-ethylmaleimide and high
concentrations of zinc chloride. {ECO:0000250}.
-!- SUBUNIT: Monomer or homodimer (By similarity). Interacts with
EPB41L3; this inhibits methylation of target proteins. Interacts
with the 40S ribosomal protein RPS2. {ECO:0000250,
ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:21059412,
ECO:0000269|Ref.16}.
-!- INTERACTION:
Q14524:SCN5A; NbExp=2; IntAct=EBI-2809009, EBI-726858;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O60678-1; Sequence=Displayed;
Name=2;
IsoId=O60678-2; Sequence=VSP_040330;
Note=No experimental confirmation available.;
-!- DOMAIN: The zinc-finger is responsible for substrate specificity.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
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EMBL; AK300591; BAG62289.1; -; mRNA.
EMBL; AC025972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC037544; AAH37544.1; -; mRNA.
EMBL; BC064831; AAH64831.1; -; mRNA.
EMBL; AF059531; AAC39837.1; -; mRNA.
CCDS; CCDS44554.1; -. [O60678-2]
CCDS; CCDS7853.1; -. [O60678-1]
RefSeq; NP_005779.1; NM_005788.3.
UniGene; Hs.152337; -.
PDB; 2FYT; X-ray; 2.00 A; A=211-531.
PDB; 3SMQ; X-ray; 2.00 A; A=211-531.
PDB; 4HSG; X-ray; 2.30 A; A=211-531.
PDB; 4QQN; X-ray; 2.08 A; A=211-531.
PDB; 4RYL; X-ray; 2.10 A; A=211-531.
PDBsum; 2FYT; -.
PDBsum; 3SMQ; -.
PDBsum; 4HSG; -.
PDBsum; 4QQN; -.
PDBsum; 4RYL; -.
ProteinModelPortal; O60678; -.
SMR; O60678; -.
BioGrid; 115491; 46.
IntAct; O60678; 16.
MINT; MINT-6803908; -.
STRING; 9606.ENSP00000331879; -.
BindingDB; O60678; -.
ChEMBL; CHEMBL5891; -.
DrugBank; DB01752; S-Adenosyl-L-Homocysteine.
GuidetoPHARMACOLOGY; 1254; -.
iPTMnet; O60678; -.
PhosphoSitePlus; O60678; -.
BioMuta; PRMT3; -.
EPD; O60678; -.
MaxQB; O60678; -.
PaxDb; O60678; -.
PeptideAtlas; O60678; -.
PRIDE; O60678; -.
DNASU; 10196; -.
Ensembl; ENST00000331079; ENSP00000331879; ENSG00000185238.
GeneID; 10196; -.
KEGG; hsa:10196; -.
UCSC; uc001mqb.4; human. [O60678-1]
CTD; 10196; -.
DisGeNET; 10196; -.
EuPathDB; HostDB:ENSG00000185238.12; -.
GeneCards; PRMT3; -.
HGNC; HGNC:30163; PRMT3.
HPA; CAB022083; -.
HPA; HPA007832; -.
MIM; 603190; gene.
neXtProt; NX_O60678; -.
PharmGKB; PA29462; -.
eggNOG; KOG1499; Eukaryota.
eggNOG; ENOG410XQYH; LUCA.
HOGENOM; HOG000198521; -.
HOVERGEN; HBG001793; -.
InParanoid; O60678; -.
KO; K11436; -.
OrthoDB; EOG091G0ADC; -.
PhylomeDB; O60678; -.
TreeFam; TF323587; -.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-8876725; Protein methylation.
SABIO-RK; O60678; -.
ChiTaRS; PRMT3; human.
EvolutionaryTrace; O60678; -.
GeneWiki; PRMT3; -.
GenomeRNAi; 10196; -.
PRO; PR:O60678; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000185238; -.
CleanEx; HS_PRMT3; -.
ExpressionAtlas; O60678; baseline and differential.
Genevisible; O60678; HS.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005840; C:ribosome; IEA:Ensembl.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0016274; F:protein-arginine N-methyltransferase activity; TAS:Reactome.
GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IBA:GO_Central.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0006479; P:protein methylation; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Metal-binding; Methyltransferase; Phosphoprotein;
Polymorphism; Reference proteome; S-adenosyl-L-methionine;
Transferase; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 531 Protein arginine N-methyltransferase 3.
/FTId=PRO_0000212326.
DOMAIN 217 531 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
ZN_FING 48 71 C2H2-type.
ACT_SITE 329 329 {ECO:0000250}.
ACT_SITE 338 338 {ECO:0000250}.
BINDING 230 230 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 239 239 S-adenosyl-L-methionine.
BINDING 263 263 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 285 285 S-adenosyl-L-methionine.
BINDING 314 314 S-adenosyl-L-methionine.
SITE 87 87 Not phosphorylated.
{ECO:0000269|PubMed:21059412}.
MOD_RES 2 2 N-acetylcysteine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21059412}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21059412}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 11 99 GRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCL
FCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKL
INFIRLK -> YSHLLKKHFHTVSLSISLILTAWFINM
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040330.
VARIANT 440 440 L -> V (in dbSNP:rs3758805).
/FTId=VAR_024584.
VARIANT 470 470 S -> C (in dbSNP:rs11025585).
/FTId=VAR_030943.
VARIANT 508 508 S -> N (in dbSNP:rs6483700).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9642256}.
/FTId=VAR_024585.
MUTAGEN 87 87 Y->C: Markedly reduced affinity for RPS2.
{ECO:0000269|PubMed:21059412}.
MUTAGEN 87 87 Y->E: Markedly reduced affinity for RPS2.
{ECO:0000269|PubMed:21059412}.
MUTAGEN 87 87 Y->F: No effect on interaction with RPS2.
{ECO:0000269|PubMed:21059412}.
CONFLICT 21 21 L -> E (in Ref. 4; AAC39837).
{ECO:0000305}.
CONFLICT 103 103 V -> F (in Ref. 1; BAG62289).
{ECO:0000305}.
CONFLICT 510 510 K -> R (in Ref. 1; BAG62289).
{ECO:0000305}.
HELIX 223 225 {ECO:0000244|PDB:2FYT}.
HELIX 227 234 {ECO:0000244|PDB:2FYT}.
HELIX 237 249 {ECO:0000244|PDB:2FYT}.
HELIX 251 253 {ECO:0000244|PDB:2FYT}.
TURN 254 256 {ECO:0000244|PDB:2FYT}.
STRAND 258 263 {ECO:0000244|PDB:2FYT}.
HELIX 268 275 {ECO:0000244|PDB:2FYT}.
STRAND 279 287 {ECO:0000244|PDB:2FYT}.
HELIX 289 299 {ECO:0000244|PDB:2FYT}.
TURN 303 305 {ECO:0000244|PDB:2FYT}.
STRAND 306 311 {ECO:0000244|PDB:2FYT}.
TURN 313 315 {ECO:0000244|PDB:2FYT}.
STRAND 319 321 {ECO:0000244|PDB:3SMQ}.
STRAND 323 328 {ECO:0000244|PDB:2FYT}.
TURN 336 338 {ECO:0000244|PDB:2FYT}.
HELIX 340 351 {ECO:0000244|PDB:2FYT}.
STRAND 352 360 {ECO:0000244|PDB:2FYT}.
STRAND 362 370 {ECO:0000244|PDB:2FYT}.
HELIX 373 379 {ECO:0000244|PDB:2FYT}.
HELIX 381 384 {ECO:0000244|PDB:2FYT}.
HELIX 392 394 {ECO:0000244|PDB:2FYT}.
HELIX 395 398 {ECO:0000244|PDB:2FYT}.
STRAND 403 405 {ECO:0000244|PDB:2FYT}.
HELIX 409 411 {ECO:0000244|PDB:2FYT}.
STRAND 417 423 {ECO:0000244|PDB:2FYT}.
TURN 424 426 {ECO:0000244|PDB:2FYT}.
HELIX 429 432 {ECO:0000244|PDB:2FYT}.
STRAND 433 442 {ECO:0000244|PDB:2FYT}.
STRAND 446 459 {ECO:0000244|PDB:2FYT}.
STRAND 467 470 {ECO:0000244|PDB:2FYT}.
STRAND 482 493 {ECO:0000244|PDB:2FYT}.
STRAND 498 507 {ECO:0000244|PDB:2FYT}.
STRAND 514 521 {ECO:0000244|PDB:2FYT}.
STRAND 524 530 {ECO:0000244|PDB:2FYT}.
SEQUENCE 531 AA; 59876 MW; D02159E2BEDBE7B9 CRC64;
MCSLASGATG GRGAVENEED LPELSDSGDE AAWEDEDDAD LPHGKQQTPC LFCNRLFTSA
EETFSHCKSE HQFNIDSMVH KHGLEFYGYI KLINFIRLKN PTVEYMNSIY NPVPWEKEEY
LKPVLEDDLL LQFDVEDLYE PVSVPFSYPN GLSENTSVVE KLKHMEARAL SAEAALARAR
EDLQKMKQFA QDFVMHTDVR TCSSSTSVIA DLQEDEDGVY FSSYGHYGIH EEMLKDKIRT
ESYRDFIYQN PHIFKDKVVL DVGCGTGILS MFAAKAGAKK VLGVDQSEIL YQAMDIIRLN
KLEDTITLIK GKIEEVHLPV EKVDVIISEW MGYFLLFESM LDSVLYAKNK YLAKGGSVYP
DICTISLVAV SDVNKHADRI AFWDDVYGFK MSCMKKAVIP EAVVEVLDPK TLISEPCGIK
HIDCHTTSIS DLEFSSDFTL KITRTSMCTA IAGYFDIYFE KNCHNRVVFS TGPQSTKTHW
KQTVFLLEKP FSVKAGEALK GKVTVHKSKK DPRSLTVTLT LNNSTQTYGL Q


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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
EIAAB31135 L-isoaspartyl protein carboxyl methyltransferase,Mouse,Mus musculus,Pcmt1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspa
EIAAB31136 Bos taurus,Bovine,L-isoaspartyl protein carboxyl methyltransferase,PCMT1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspar
EIAAB31133 Homo sapiens,Human,L-isoaspartyl protein carboxyl methyltransferase,PCMT1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspa
EIAAB31132 Chicken,Gallus gallus,L-isoaspartyl protein carboxyl methyltransferase,PCMT1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-a
EIAAB31137 L-isoaspartyl protein carboxyl methyltransferase,PCMT1,Pig,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspartate) O-methyl
EIAAB31134 L-isoaspartyl protein carboxyl methyltransferase,Pcmt1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspartate) O-methyltran
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
E2223Rb ELISA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus 96T
U2223Rb CLIA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus, 96T
E2223Rb Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus,Rabbit
E2223h Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT
E2223m Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt
U2223m CLIA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Tem 96T
U2223m CLIA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt 96T
E2223h ELISA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T
E2223h ELISA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T
U2223h CLIA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T
E2223m ELISA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt 96T
U2223Rb CLIA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus,Rabbi 96T
U2223h CLIA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T


 

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