CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008987
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein arginine N-methyltransferase 2 
Protein Synonyms/Alias
 Histone-arginine N-methyltransferase PRMT2 
Gene Name
 PRMT2 
Gene Synonyms/Alias
 HMT1; HRMT1L1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
56LSFLRGEKILILRQTubiquitination[1]
86IPANHVGKHVDEYDPubiquitination[1]
124ADQPRTTKYHSVILQubiquitination[1]
427TSQKVGEKVFPIWR*ubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1- dependent manner). May be involved in growth regulation. 
Sequence Annotation
 DOMAIN 30 89 SH3.
 REGION 83 207 Interaction with RB1 (By similarity).
 REGION 133 275 Interaction with ESR1.
 ACT_SITE 211 211 By similarity.
 ACT_SITE 220 220 By similarity.
 BINDING 112 112 S-adenosyl-L-methionine (By similarity).
 BINDING 121 121 S-adenosyl-L-methionine (By similarity).
 BINDING 145 145 S-adenosyl-L-methionine; via carbonyl
 BINDING 168 168 S-adenosyl-L-methionine (By similarity).
 BINDING 197 197 S-adenosyl-L-methionine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine; SH3 domain; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 433 AA 
Protein Sequence
MATSGDCPRS ESQGEEPAEC SEAGLLQEGV QPEEFVAIAD YAATDETQLS FLRGEKILIL 60
RQTTADWWWG ERAGCCGYIP ANHVGKHVDE YDPEDTWQDE EYFGSYGTLK LHLEMLADQP 120
RTTKYHSVIL QNKESLTDKV ILDVGCGTGI ISLFCAHYAR PRAVYAVEAS EMAQHTGQLV 180
LQNGFADIIT VYQQKVEDVV LPEKVDVLVS EWMGTCLLFE FMIESILYAR DAWLKEDGVI 240
WPTMAALHLV PCSADKDYRS KVLFWDNAYE FNLSALKSLA VKEFFSKPKY NHILKPEDCL 300
SEPCTILQLD MRTVQISDLE TLRGELRFDI RKAGTLHGFT AWFSVHFQSL QEGQPPQVLS 360
TGPFHPTTHW KQTLFMMDDP VPVHTGDVVT GSVVLQRNPV WRRHMSVALS WAVTSRQDPT 420
SQKVGEKVFP IWR 433 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0030331; F:estrogen receptor binding; IDA:UniProtKB.
 GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:UniProtKB.
 GO:0004871; F:signal transducer activity; TAS:ProtInc.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0048588; P:developmental cell growth; ISS:UniProtKB.
 GO:0097194; P:execution phase of apoptosis; IDA:UniProtKB.
 GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
 GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB. 
Interpro
 IPR025799; Arg_MeTrfase.
 IPR025798; Arg_MeTrfase_PMTR2.
 IPR001452; SH3_domain. 
Pfam
 PF05185; PRMT5
 PF00018; SH3_1 
SMART
 SM00326; SH3 
PROSITE
 PS50002; SH3 
PRINTS
 PR00452; SH3DOMAIN.