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Protein arginine N-methyltransferase 2 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT2)

 ANM2_XENLA              Reviewed;         432 AA.
D9IVE5;
08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 2.
22-NOV-2017, entry version 39.
RecName: Full=Protein arginine N-methyltransferase 2;
EC=2.1.1.319 {ECO:0000250|UniProtKB:P55345};
AltName: Full=Histone-arginine N-methyltransferase PRMT2;
Name=prmt2;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CTNNB1.
PubMed=20708585; DOI=10.1016/j.devcel.2010.07.007;
Blythe S.A., Cha S.-W., Tadjuidje E., Heasman J., Klein P.S.;
"beta-Catenin primes organizer gene expression by recruiting a histone
H3 arginine 8 methyltransferase, Prmt2.";
Dev. Cell 19:220-231(2010).
-!- FUNCTION: Arginine methyltransferase that methylates the guanidino
nitrogens of arginyl residues in proteins such as histones.
Involved in growth regulation (By similarity). Involved in
embryonic dorsal development. {ECO:0000250,
ECO:0000269|PubMed:20708585}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + [protein]-L-
arginine = 2 S-adenosyl-L-homocysteine + [protein]-
N(omega),N(omega)-dimethyl-L-arginine.
{ECO:0000250|UniProtKB:P55345}.
-!- SUBUNIT: Interacts with ctnnb1. {ECO:0000269|PubMed:20708585}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
-!- SEQUENCE CAUTION:
Sequence=ADK11289.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; HM205111; ADK11289.1; ALT_INIT; mRNA.
RefSeq; NP_001181877.1; NM_001194948.1.
UniGene; Xl.86744; -.
ProteinModelPortal; D9IVE5; -.
SMR; D9IVE5; -.
GeneID; 100499207; -.
KEGG; xla:100499207; -.
CTD; 100499207; -.
Xenbase; XB-GENE-6486904; prmt2.
KO; K11435; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; ISS:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0048588; P:developmental cell growth; IMP:UniProtKB.
GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISS:UniProtKB.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF07653; SH3_2; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Cytoplasm; Methyltransferase; Nucleus; S-adenosyl-L-methionine;
SH3 domain; Transferase.
CHAIN 1 432 Protein arginine N-methyltransferase 2.
/FTId=PRO_0000404155.
DOMAIN 29 88 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 101 405 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
ACT_SITE 213 213 {ECO:0000250}.
ACT_SITE 222 222 {ECO:0000250}.
BINDING 114 114 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 123 123 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 147 147 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
BINDING 170 170 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 199 199 S-adenosyl-L-methionine. {ECO:0000250}.
SEQUENCE 432 AA; 49525 MW; 55CF6D6414BB7724 CRC64;
MESSSECSSI SDFQDSTEGD DANTLPENLC MREYVVICDY VATDNTQLSL CSGDKVLLLN
AVSQDWWWVN HNGTCGYVPA SHLHDALNEQ EDTEVNDPWQ DEEYYGSYKT LKLHLEMLSD
VPRTMTYQNV ILKNSSSLCG KHILDLGCGT GIISFFCAKF AQPEAVYAVE ASKIAEQTCR
LVEQNGISSL VHVIRQQAEE LDLPTKVDVL VSEWMGTCLL FEFMLESVLQ ARDRWLKEDG
VMWPSTACIH LVPCSAYKEY SNKVLFWDNP YQLDFSLLKP PATKEFFAKP QPDYILQPED
CLSEPCTLFH LNLKTLQVAE LERMNCDFTF LVHTNGLLHG FTAWFSVQFE NLEEQGHLEL
NTGPFSPLTH WKHTLFMLDE PLQVQKRDKI SGSVVFERNS VWRRHMSVTL SWVISRELKM
QKVGCKVFPI WR


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